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866  structures 886  species 26  interactions 23726  sequences 823  architectures

Family: PDZ (PF00595)

Summary: PDZ domain (Also known as DHR or GLGF)

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PDZ domain Edit Wikipedia article

PDZ domain 2DC2.png
Molecular structure of the PDZ domain included in the human GOPC (Golgi-associated PDZ and coiled-coil motif-containing protein) protein
Identifiers
Symbol PDZ
Pfam PF00595
InterPro IPR001478
SMART PDZ
PROSITE PDOC50106
SCOP 1lcy
SUPERFAMILY 1lcy
CDD cd00136

The PDZ domain is a common structural domain of 80-90 amino-acids found in the signaling proteins of bacteria, yeast, plants, viruses[1] and animals.[2] Proteins containing PDZ domains play a key role in anchoring receptor proteins in the membrane to cytoskeletal components. PDZ is an acronym combining the first letters of three proteins — post synaptic density protein (PSD95), Drosophila disc large tumor suppressor (Dlg1), and zonula occludens-1 protein (zo-1) — which were first discovered to share the domain.[3] PDZ domains have previously been referred to as DHR (Dlg homologous region)[4] or GLGF (glycine-leucine-glycine-phenylalanine) domains.[5] Proteins with these domains help hold together and organize signaling complexes at cellular membranes. Protein domains, connected by intrinsically disordered flexible linker regions, induce long-range allostery via protein domain dynamics.[6] PDZ domains also play a highly significant role in the anchoring of cell surface receptors (such as CFTR[disambiguation needed] and FZD7) to the actin cytoskeleton via mediators like NHERF and ezrin. [7]

In general PDZ domains bind to a short region of the C-terminus of other specific proteins. These short regions bind to the PDZ domain by beta sheet augmentation. This means that the beta sheet in the PDZ domain is extended by the addition of a further beta strand from the tail of the binding partner protein.[8]

Origins of discovery

PDZ is an acronym derived from the names of the first proteins in which the domain was observed. Post-synaptic density protein 95 (PSD-95) is a synaptic protein found only in the brain[5] Drosophila disc large tumor suppressor (Dlg1) and zona occludens 1 (ZO-1) both play an important role at junctions and in cell signaling complexes.[9] Since the discovery of PDZ domains more than 20 years ago, researchers have successfully identified hundreds of PDZ domains. The first published use of the phrase “PDZ domain” was not in a paper, but a letter. In September 1995, Dr. Mary B. Kennedy of the California Institute of Technology wrote a letter of correction to Trends in Biomedical Sciences.[10] Earlier that year, another set of scientists had claimed to discover a new protein domain which they called a DHR domain.[11] Dr. Kennedy refuted that her lab had previously described the exact same domain as a series of “GLGF repeats”.[5] She continued to explain that in order to “better reflect the origin and distribution of the domain,” the new title of the domain would be changed. Thus, the name “PDZ domain” was introduced to the world.

Functions

Any protein may have one or several PDZ domains, which can be identical or unique (see figure to right). Different PDZ domains can have different roles, each binding a different part of the target protein or a different protein altogether.[12] In this way, PDZ domains play a vital role in organizing and maintaining complex scaffolding formations.

An example of a protein (GRIP) with seven PDZ domains.

PDZ domains are found in many different contexts and diverse proteins, but all assist in localization of cellular elements. PDZ domains are primarily involved in anchoring receptor proteins to the cytoskeleton. In any cell, an important responsibility is to get the right components—proteins and other molecules—in the right place at the right time. In the neuron, making sense of neurotransmitter activity requires specific receptors to be located in the lipid membrane at the synapse. PDZ domains are a critical part of this receptor localization process.[13] Proteins with PDZ domains generally associate with both the C-terminus of the receptor and cytoskeletal elements in order to anchor the receptor to the cytoskeleton and keep it in place.[12][14] Without such an interaction, receptors would diffuse out of the synapse due to the fluid nature of the lipid membrane.

PDZ domains are also utilized to localize elements other than receptor proteins. In the human brain, nitric oxide often acts in the synapse to modify cGMP levels in response to NMDA receptor activation.[15] In order to ensure a favorable spatial arrangements, neuronal nitric oxide synthase (nNOS) is brought close to NMDA receptors via interactions with PDZ domains on PSD-95, which concurrently binds nNOS and NMDA receptors.[14] With nNOS located closely to NMDA receptors, it will be activated immediately after calcium ions begin entering the cell. Instances such as this illustrate how PDZ domains can lead to greater signaling efficiency than diffusion alone.

Another interesting role played by PDZ domains involves regulation of the sorting pathway of endocytosed receptor proteins. A PDZ domain on the EBP50 protein binds to the C-terminus of the beta-2 adrenergic receptor (ß2-AR). EBP50 also associates with a complex that connects to actin, thus serving as a link between the cytoskeleton and ß2-AR.[16] The ß2-AR receptor is eventually endocytosed, where it will either be consigned to a lysosome for degradation or recycled back to the cell membrane. Scientists have demonstrated that when the Ser-411 residue of the ß2-AR PDZ binding domain, which interacts directly with EBP50, is phosphorylated, the receptor is degraded. If Ser-411 is left unmodified, the receptor is recycled.[16] The role played by PDZ domains and their binding sites indicate a regulative relevance beyond simply receptor protein localization.

PDZ proteins

Examples of PDZ domain-containing proteins (Figure from Lee et al. 2010).[17] Proteins are indicated by black lines scaled to the length of the primary sequence of the protein. Different shapes refer to different protein domains.

PDZ domains are found in many thousands of known proteins. PDZ domain proteins are widespread in eukaryotes and eubacteria,[2] whereas there are very few examples of the protein in archaea. PDZ domains are often associated with other protein domains and these combinations allow them to carry out their specific functions. Three of the most well documented PDZ proteins are PSD-95, GRIP, and HOMER. PSD-95 is a brain synaptic protein with three PDZ domains, each with unique properties and structures that allow PSD-95 to function in many ways. In general, the first two PDZ domains interact with receptors and the third interacts with cytoskeleton-related proteins. The main receptors associated with PSD-95 are NMDA receptors. The first two PDZ domains of PSD-95 bind to the C-terminus of NMDA receptors and anchor them in the membrane at the point of neurotransmitter release.[18] The first two PDZ domains can also interact in a similar fashion with Shaker-type K+ channels.[18] A PDZ interaction between PSD-95, nNOS and syntrophin is mediated by the second PDZ domain. The third and final PDZ domain links to cysteine-rich PDZ-binding protein (CRIPT), which allows PSD-95 to associate with the cytoskeleton.[18]

Glutamate receptor interacting protein (GRIP) is a post-synaptic protein with that interacts with AMPA receptors in a fashion analogous to PSD-95 interactions with NMDA receptors. When researchers noticed apparent structural homology between the C-termini of AMPA receptors and NMDA receptors, they attempted to determine if a similar PDZ interaction was occurring.[19] A yeast two-hybrid system helped them discover that out of GRIP’s seven PDZ domains, two (domains four and five) were essential for binding of GRIP to the AMPA subunit called GluR2.[12] This interaction is vital for proper localization of AMPA receptors, which play a large part in memory storage. Other researchers discovered that domains six and seven of GRIP are responsible for connecting GRIP to a family of receptor tyrosine kinases called ephrin receptors, which are important signaling proteins.[20] A clinical study concluded that Fraser syndrome, an autosomal recessive syndrome that can cause severe deformations, can be caused by a simple mutation in GRIP.[21]

HOMER differs significantly from many known PDZ proteins, including GRIP and PSD-95. Instead of mediating receptors near ion channels, as is the case with GRIP and PSD-95, HOMER is involved in metabotropic glutamate signaling.[7] Another unique aspect of HOMER is that it only contains a single PDZ domain, which mediates interactions between HOMER and type 5 metabotropic glutamate receptor (mGluR5).[13] The single GLGF repeat on HOMER binds amino acids on the C-terminus of mGluR5. HOMER expression is measured at high levels during embryologic stages in rats, suggesting an important developmental function.[13]

Human

There are roughly 260 human PDZ domains. However, several proteins contain multiple PDZ domains, so the number of unique PDZ-containing proteins is closer to 180. Listed below are some of the better studied members of this family:

Below is a complete list:

AAG12; AHNAK; AHNAK2; AIP1; ALP; APBA1; APBA2; APBA3; ARHGAP21; ARHGAP23; ARHGEF11; ARHGEF12; CASK; CLP-36; CNKSR2; CNKSR3; CRTAM; DFNB31; DLG1; DLG2; DLG3; DLG4; DLG5; DVL1; DVL1L1; DVL2; DVL3; ERBB2IP; FRMPD1; FRMPD2; FRMPD2L1; FRMPD3; FRMPD4; GIPC1; GIPC2; GIPC3; GOPC; GRASP; GRIP1; GRIP2; HTRA1; HTRA2; HTRA3; HTRA4; IL16; INADL; KIAA1849; LDB3; LIMK1; LIMK2; LIN7A; LIN7B; LIN7C; LMO7; LNX1; LNX2; LRRC7; MAGI1; MAGI2; MAGI3; MAGIX; MAST1; MAST2; MAST3; MAST4; MCSP; MLLT4; MPDZ; MPP1; MPP2; MPP3; MPP4; MPP5; MPP6; MPP7; MYO18A;  ;NOS1; PARD3; PARD3B; PARD6A; PARD6B; PARD6G; PDLIM1; PDLIM2; PDLIM3; PDLIM4; PDLIM5; PDLIM7; PDZD11; PDZD2; PDZD3; PDZD4; PDZD5A; PDZD7; PDZD8; PDZK1; PDZRN3; PDZRN4; PICK1; PPP1R9A; PPP1R9B; PREX1; PRX; PSCDBP; PTPN13; PTPN3; PTPN4; RAPGEF2; RAPGEF6; RGS12; RGS3; RHPN1; RIL; RIMS1; RIMS2; SCN5A; SCRIB; SDCBP; SDCBP2; SHANK1; SHANK2; SHANK3; SHROOM2; SHROOM3; SHROOM4; SIPA1; SIPA1L1; SIPA1L2; SIPA1L3; SLC9A3R1; SLC9A3R2; SNTA1; SNTB1; SNTB2; SNTG1; SNTG2; SNX27; SPAL2; STXBP4; SYNJ2BP; SYNPO2; SYNPO2L; TAX1BP3; TIAM1; TIAM2; TJP1; TJP2; TJP3; TRPC4; TRPC5; USH1C; WHRN;

Virus

Tax1

References

  1. ^ Boxus M, Twizere JC, Legros S, Dewulf JF, Kettmann R, Willems L (2008). "The HTLV-1 Tax interactome". Retrovirology 5: 76. doi:10.1186/1742-4690-5-76. PMC 2533353. PMID 18702816. 
  2. ^ a b Ponting CP (February 1997). "Evidence for PDZ domains in bacteria, yeast, and plants". Protein Sci. 6 (2): 464–468. doi:10.1002/pro.5560060225. PMC 2143646. PMID 9041651. 
  3. ^ Kennedy MB (September 1995). "Origin of PDZ(DHR,GLGF) domains". Trends Biochem. Sci. 20 (9): 350. doi:10.1016/S0968-0004(00)89074-X. PMID 7482701. 
  4. ^ Ponting CP, Phillips C (March 1995). "DHR domains in syntrophins, neuronal NO synthases and other intracellular proteins". Trends Biochem. Sci. 20 (3): 102–103. doi:10.1016/S0968-0004(00)88973-2. PMID 7535955. 
  5. ^ a b c Cho KO, Hunt CA, Kennedy MB (Nov 1992). "The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein". Neuron 9 (5): 929–42. doi:10.1016/0896-6273(92)90245-9. PMID 1419001. 
  6. ^ Bu Z, Callaway DJ (2011). "Proteins MOVE! Protein dynamics and long-range allostery in cell signaling". Adv in Protein Chemistry and Structural Biology. Advances in Protein Chemistry and Structural Biology 83: 163–221. doi:10.1016/B978-0-12-381262-9.00005-7. ISBN 9780123812629. PMID 21570668. 
  7. ^ a b Ranganathan R, Ross E (1997). "PDZ domain proteins: scaffolds for signaling complexes". Curr Biol 7 (12): R770–R773. doi:10.1016/S0960-9822(06)00401-5. PMID 9382826. 
  8. ^ Cowburn D (December 1997). "Peptide recognition by PTB and PDZ domains". Curr. Opin. Struct. Biol. 7 (6): 835–838. doi:10.1016/S0959-440X(97)80155-8. PMID 9434904. 
  9. ^ Liu, Jie; Li, Juan; Ren, Yu; Liu, Peijun (2014-01-01). "DLG5 in cell polarity maintenance and cancer development". International Journal of Biological Sciences 10 (5): 543–549. doi:10.7150/ijbs.8888. ISSN 1449-2288. PMC 4046881. PMID 24910533. 
  10. ^ Kennedy, M. B. (1995-09-01). "Origin of PDZ (DHR, GLGF) domains". Trends in Biochemical Sciences 20 (9): 350. ISSN 0968-0004. PMID 7482701. 
  11. ^ Ponting, Christopher P.; Phillips, Christopher (1995-03-01). "DHR domains in syntrophins, neuronal NO synthases and other intracellular proteins". Trends in Biochemical Sciences 20 (3): 102–103. doi:10.1016/S0968-0004(00)88973-2. 
  12. ^ a b c Bristol, University of. "Bristol University | Centre for Synaptic Plasticity | AMPAR interactors". www.bristol.ac.uk. Retrieved 2015-12-03. 
  13. ^ a b c Brakeman, P. R.; Lanahan, A. A.; O'Brien, R.; Roche, K.; Barnes, C. A.; Huganir, R. L.; Worley, P. F. (1997-03-20). "Homer: a protein that selectively binds metabotropic glutamate receptors". Nature 386 (6622): 284–288. doi:10.1038/386284a0. ISSN 0028-0836. PMID 9069287. 
  14. ^ a b Doyle, D. A.; Lee, A.; Lewis, J.; Kim, E.; Sheng, M.; MacKinnon, R. (1996-06-28). "Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ". Cell 85 (7): 1067–1076. ISSN 0092-8674. PMID 8674113. 
  15. ^ Hopper, Rachel; Lancaster, Barrie; Garthwaite, John (2004-04-01). "On the regulation of NMDA receptors by nitric oxide". The European Journal of Neuroscience 19 (7): 1675–1682. doi:10.1111/j.1460-9568.2004.03306.x. ISSN 0953-816X. PMID 15078541. 
  16. ^ a b Cao, T. T.; Deacon, H. W.; Reczek, D.; Bretscher, A.; von Zastrow, M. (1999-09-16). "A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor". Nature 401 (6750): 286–290. doi:10.1038/45816. ISSN 0028-0836. PMID 10499588. 
  17. ^ Lee HJ, Zheng JJ (2010). "PDZ domains and their binding partners: structure, specificity, and modification". Cell Commun. Signal 8: 8. doi:10.1186/1478-811X-8-8. PMC 2891790. PMID 20509869. 
  18. ^ a b c Niethammer, M.; Valtschanoff, J. G.; Kapoor, T. M.; Allison, D. W.; Weinberg, R. J.; Craig, A. M.; Sheng, M. (1998-04-01). "CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90". Neuron 20 (4): 693–707. ISSN 0896-6273. PMID 9581762. 
  19. ^ Dong, H.; O'Brien, R. J.; Fung, E. T.; Lanahan, A. A.; Worley, P. F.; Huganir, R. L. (1997-03-20). "GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors". Nature 386 (6622): 279–284. doi:10.1038/386279a0. ISSN 0028-0836. PMID 9069286. 
  20. ^ Torres, Richard; Firestein, Bonnie L; Dong, Hualing; Staudinger, Jeff; Olson, Eric N; Huganir, Richard L; Bredt, David S; Gale, Nicholas W; Yancopoulos, George D (1998-12-01). "PDZ Proteins Bind, Cluster, and Synaptically Colocalize with Eph Receptors and Their Ephrin Ligands". Neuron 21 (6): 1453–1463. doi:10.1016/S0896-6273(00)80663-7. 
  21. ^ Vogel, Maartje J.; van Zon, Patrick; Brueton, Louise; Gijzen, Marleen; van Tuil, Marc C.; Cox, Phillip; Schanze, Denny; Kariminejad, Ariana; Ghaderi-Sohi, Siavash (2012-05-01). "Mutations in GRIP1 cause Fraser syndrome". Journal of Medical Genetics 49 (5): 303–306. doi:10.1136/jmedgenet-2011-100590. ISSN 1468-6244. PMID 22510445. 
  22. ^ Jemth P, Gianni S (July 2007). "PDZ domains: folding and binding". Biochemistry 46 (30): 8701–8708. doi:10.1021/bi7008618. PMID 17620015. 

Further reading

  • Ponting CP, Phillips C, Davies KE, Blake DJ (June 1997). "PDZ domains: targeting signalling molecules to sub-membranous sites". BioEssays 19 (6): 469–479. doi:10.1002/bies.950190606. PMID 9204764. 
  • Doyle DA, Lee A, Lewis J, Kim E, Sheng M, MacKinnon R (June 1996). "Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ". Cell 85 (7): 1067–1076. doi:10.1016/S0092-8674(00)81307-0. PMID 8674113. 

External links

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

PDZ domain (Also known as DHR or GLGF) Provide feedback

PDZ domains are found in diverse signaling proteins.

Literature references

  1. Ponting CP, Phillips C, Davies KE, Blake DJ , Bioessays 1997;19:469-479.: PDZ domains: targeting signalling molecules to sub-membranous sites. PUBMED:9204764 EPMC:9204764

  2. Doyle DA, Lee A, Lewis J, Kim E, Sheng M, MacKinnon R; , Cell. 1996;85:1067-1076.: Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. PUBMED:8674113 EPMC:8674113

  3. Ponting CP; , Protein Sci 1997;6:464-468.: Evidence for PDZ domains in bacteria, yeast, and plants. PUBMED:9041651 EPMC:9041651

  4. Ernst A, Sazinsky SL, Hui S, Currell B, Dharsee M, Seshagiri S, Bader GD, Sidhu SS;, Sci Signal. 2009;2:ra50.: Rapid evolution of functional complexity in a domain family. PUBMED:19738200 EPMC:19738200


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001478

PDZ domains (also known as Discs-large homologous regions (DHR) or GLGF)) are found in diverse signalling proteins in bacteria, yeasts, plants, insects and vertebrates [PUBMED:9041651, PUBMED:9204764]. PDZ domains can occur in one or multiple copies and are nearly always found in cytoplasmic proteins. They bind either the carboxyl-terminal sequences of proteins or internal peptide sequences [PUBMED:9204764]. In most cases, interaction between a PDZ domain and its target is constitutive, with a binding affinity of 1 to 10 microns. However, agonist-dependent activation of cell surface receptors is sometimes required to promote interaction with a PDZ protein. PDZ domain proteins are frequently associated with the plasma membrane, a compartment where high concentrations of phosphatidylinositol 4,5-bisphosphate (PIP2) are found. Direct interaction between PIP2 and a subset of class II PDZ domains (syntenin, CASK, Tiam-1) has been demonstrated.

PDZ domains consist of 80 to 90 amino acids comprising six beta-strands (beta-A to beta-F) and two alpha-helices, A and B, compactly arranged in a globular structure. Peptide binding of the ligand takes place in an elongated surface groove as an anti-parallel beta-strand interacts with the beta-B strand and the B helix. The structure of PDZ domains allows binding to a free carboxylate group at the end of a peptide through a carboxylate-binding loop between the beta-A and beta-B strands.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan PDZ-like (CL0466), which has the following description:

This superfamily comprises families of PDZ domains, which are peptide binding sites.

The clan contains the following 5 members:

GRASP55_65 PDZ PDZ_1 PDZ_2 Tricorn_PDZ

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(44)
Full
(23726)
Representative proteomes UniProt
(44717)
NCBI
(154153)
Meta
(4927)
RP15
(4882)
RP35
(8149)
RP55
(14746)
RP75
(19690)
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Key: ✓ available, x not generated, not available.

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  Seed
(44)
Full
(23726)
Representative proteomes UniProt
(44717)
NCBI
(154153)
Meta
(4927)
RP15
(4882)
RP35
(8149)
RP55
(14746)
RP75
(19690)
Alignment:
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Sequence:
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  Seed
(44)
Full
(23726)
Representative proteomes UniProt
(44717)
NCBI
(154153)
Meta
(4927)
RP15
(4882)
RP35
(8149)
RP55
(14746)
RP75
(19690)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: [1]
Previous IDs: none
Type: Domain
Author: Bateman A
Number in seed: 44
Number in full: 23726
Average length of the domain: 81.00 aa
Average identity of full alignment: 24 %
Average coverage of the sequence by the domain: 15.71 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.0 27.0
Trusted cut-off 27.0 27.0
Noise cut-off 26.9 26.9
Model length: 82
Family (HMM) version: 21
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

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Interactions

There are 26 interactions for this family. More...

MAGUK_N_PEST PDZ_assoc Metallophos Trypsin Ras SH3_2 PDZ Lys Trypsin Porin_1 Cadherin_C EB1_binding Peptidase_M50 Trypsin_2 NMDAR2_C SH3_2 DUF4136 MAGUK_N_PEST Syndecan PDZ_assoc Porin_1 Peptidase_M50 EBP50_C SAM_1 Trypsin_2 PID

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the PDZ domain has been found. There are 866 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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