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9  structures 46  species 0  interactions 96  sequences 3  architectures

Family: ecTbetaR2 (PF08917)

Summary: Transforming growth factor beta receptor 2 ectodomain

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This is the Wikipedia entry entitled "TGF beta receptor 2". More...

TGF beta receptor 2 Edit Wikipedia article

Transforming growth factor, beta receptor II (70/80kDa)
Protein TGFBR2 PDB 1ktz.png
PDB rendering based on 1ktz.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols TGFBR2 ; AAT3; FAA3; LDS1B; LDS2; LDS2B; MFS2; RIIC; TAAD2; TGFR-2; TGFbeta-RII
External IDs OMIM190182 MGI98729 HomoloGene2435 ChEMBL: 4267 GeneCards: TGFBR2 Gene
EC number 2.7.11.30
RNA expression pattern
PBB GE TGFBR2 208944 at tn.png
PBB GE TGFBR2 207334 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 7048 21813
Ensembl ENSG00000163513 ENSMUSG00000032440
UniProt P37173 Q62312
RefSeq (mRNA) NM_001024847 NM_009371
RefSeq (protein) NP_001020018 NP_033397
Location (UCSC) Chr 3:
30.65 – 30.74 Mb
Chr 9:
116.09 – 116.18 Mb
PubMed search [1] [2]

Transforming growth factor, beta receptor II (70/80kDa) is a TGF beta receptor. TGFBR2 is its human gene.

It is a tumor suppressor gene.[1]

This gene encodes a member of the Ser/Thr protein kinase family and the TGFB receptor subfamily. The encoded protein is a transmembrane protein that has a protein kinase domain, forms a heterodimeric complex with another receptor protein, and binds TGF-beta. This receptor/ligand complex phosphorylates proteins, which then enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation. Mutations in this gene have been associated with Marfan syndrome, Loeys-Deitz aortic aneurysm syndrome, Osler-Weber-Rendu syndrome, and the development of various types of tumors. Alternatively spliced transcript variants encoding different isoforms have been characterized.[2]

Interactions

TGF beta receptor 2 has been shown to interact with Cyclin B2,[3] TGF beta receptor 1,[4][5] Transforming growth factor, beta 3,[6][7][8][9] AP2B1,[10] Endoglin,[8][11] Heat shock protein 90kDa alpha (cytosolic), member A1[12] and STRAP.[13][14]

Domain architecture

Transforming growth factor beta receptor 2 ectodomain
PDB 1m9z EBI.jpg
crystal structure of human tgf-beta type ii receptor ligand binding domain
Identifiers
Symbol ecTbetaR2
Pfam PF08917
InterPro IPR015013

TGF beta receptor 2 consists of a C-terminal protein kinase domain and an N-terminal ectodomain. The ectodomain consists of a compact fold containing nine beta-strands and a single helix stabilised by a network of six intra strand disulphide bonds. The folding topology includes a central five-stranded antiparallel beta-sheet, eight-residues long at its centre, covered by a second layer consisting of two segments of two-stranded antiparallel beta-sheets (beta1-beta4, beta3-beta9).[7]

See also

External links

References

  1. ^ "TGFBR2 - transforming growth factor, beta receptor II (70/80kDa) - Genetics Home Reference". Retrieved 2008-09-07. 
  2. ^ "Entrez Gene: TGFBR2 transforming growth factor, beta receptor II (70/80kDa)". 
  3. ^ Liu, J H; Wei S; Burnette P K; Gamero A M; Hutton M; Djeu J Y (January 1999). "Functional association of TGF-beta receptor II with cyclin B". Oncogene (ENGLAND) 18 (1): 269–75. doi:10.1038/sj.onc.1202263. ISSN 0950-9232. PMID 9926943. 
  4. ^ Kawabata, M; Chytil A; Moses H L (March 1995). "Cloning of a novel type II serine/threonine kinase receptor through interaction with the type I transforming growth factor-beta receptor". J. Biol. Chem. (UNITED STATES) 270 (10): 5625–30. doi:10.1074/jbc.270.10.5625. ISSN 0021-9258. PMID 7890683. 
  5. ^ Razani, B; Zhang X L; Bitzer M; von Gersdorff G; Böttinger E P; Lisanti M P (March 2001). "Caveolin-1 regulates transforming growth factor (TGF)-beta/SMAD signaling through an interaction with the TGF-beta type I receptor". J. Biol. Chem. (United States) 276 (9): 6727–38. doi:10.1074/jbc.M008340200. ISSN 0021-9258. PMID 11102446. 
  6. ^ De Crescenzo, Gregory; Pham Phuong L, Durocher Yves, O'Connor-McCourt Maureen D (May 2003). "Transforming growth factor-beta (TGF-beta) binding to the extracellular domain of the type II TGF-beta receptor: receptor capture on a biosensor surface using a new coiled-coil capture system demonstrates that avidity contributes significantly to high affinity binding". J. Mol. Biol. (England) 328 (5): 1173–83. doi:10.1016/S0022-2836(03)00360-7. ISSN 0022-2836. PMID 12729750. 
  7. ^ a b Hart, P John; Deep Shashank; Taylor Alexander B; Shu Zhanyong; Hinck Cynthia S; Hinck Andrew P (March 2002). "Crystal structure of the human TbetaR2 ectodomain--TGF-beta3 complex". Nat. Struct. Biol. (United States) 9 (3): 203–8. doi:10.1038/nsb766. ISSN 1072-8368. PMID 11850637. 
  8. ^ a b Barbara, N P; Wrana J L; Letarte M (January 1999). "Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily". J. Biol. Chem. (UNITED STATES) 274 (2): 584–94. doi:10.1074/jbc.274.2.584. ISSN 0021-9258. PMID 9872992. 
  9. ^ Rotzer, D; Roth M; Lutz M; Lindemann D; Sebald W; Knaus P (February 2001). "Type III TGF-beta receptor-independent signalling of TGF-beta2 via TbetaRII-B, an alternatively spliced TGF-beta type II receptor". EMBO J. (England) 20 (3): 480–90. doi:10.1093/emboj/20.3.480. ISSN 0261-4189. PMC 133482. PMID 11157754. 
  10. ^ Yao, Diying; Ehrlich Marcelo; Henis Yoav I; Leof Edward B (November 2002). "Transforming growth factor-beta receptors interact with AP2 by direct binding to beta2 subunit". Mol. Biol. Cell (United States) 13 (11): 4001–12. doi:10.1091/mbc.02-07-0104. ISSN 1059-1524. PMC 133610. PMID 12429842. 
  11. ^ Guerrero-Esteo, Mercedes; Sanchez-Elsner Tilman, Letamendia Ainhoa, Bernabeu Carmelo (August 2002). "Extracellular and cytoplasmic domains of endoglin interact with the transforming growth factor-beta receptors I and II". J. Biol. Chem. (United States) 277 (32): 29197–209. doi:10.1074/jbc.M111991200. ISSN 0021-9258. PMID 12015308. 
  12. ^ Wrighton, Katharine H; Lin Xia; Feng Xin-Hua (July 2008). "Critical regulation of TGFbeta signaling by Hsp90". Proc. Natl. Acad. Sci. U.S.A. (United States) 105 (27): 9244–9. doi:10.1073/pnas.0800163105. PMC 2453700. PMID 18591668. 
  13. ^ Datta, P K; Chytil A; Gorska A E; Moses H L (Dec 1998). "Identification of STRAP, a novel WD domain protein in transforming growth factor-beta signaling". J. Biol. Chem. (UNITED STATES) 273 (52): 34671–4. doi:10.1074/jbc.273.52.34671. ISSN 0021-9258. PMID 9856985. 
  14. ^ Datta, P K; Moses H L (May 2000). "STRAP and Smad7 synergize in the inhibition of transforming growth factor beta signaling". Mol. Cell. Biol. (UNITED STATES) 20 (9): 3157–67. doi:10.1128/MCB.20.9.3157-3167.2000. ISSN 0270-7306. PMC 85610. PMID 10757800. 


This article incorporates text from the public domain Pfam and InterPro IPR015013

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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.

Transforming growth factor beta receptor 2 ectodomain Provide feedback

The Transforming growth factor beta receptor 2 ectodomain is a compact fold consisting of nine beta-strands and a single helix stabilised by a network of six intra strand disulphide bonds. The folding topology includes a central five-stranded antiparallel beta-sheet, eight-residues long at its centre, covered by a second layer consisting of two segments of two-stranded antiparallel beta-sheets (beta1-beta4, beta3-beta9) [1].

Literature references

  1. Hart PJ, Deep S, Taylor AB, Shu Z, Hinck CS, Hinck AP; , Nat Struct Biol. 2002;9:203-208.: Crystal structure of the human TbetaR2 ectodomain--TGF-beta3 complex. PUBMED:11850637 EPMC:11850637


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR015013

The Transforming growth factor beta receptor 2 ectodomain is a compact fold consisting of nine beta-strands and a single helix stabilised by a network of six intra strand disulphide bonds. The folding topology includes a central five-stranded antiparallel beta-sheet, eight-residues long at its centre, covered by a second layer consisting of two segments of two-stranded antiparallel beta-sheets (beta1-beta4, beta3-beta9) [PUBMED:11850637].

Gene Ontology

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Domain organisation

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Alignments

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RP35
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RP55
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RP75
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(6)
Full
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Representative proteomes NCBI
(87)
Meta
(0)
RP15
(1)
RP35
(7)
RP55
(18)
RP75
(38)
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External links

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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: pdb_1ktz
Previous IDs: none
Type: Domain
Author: Mistry J, Sammut SJ
Number in seed: 6
Number in full: 96
Average length of the domain: 110.20 aa
Average identity of full alignment: 54 %
Average coverage of the sequence by the domain: 22.61 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 25.0 36.2
Noise cut-off 21.5 22.8
Model length: 118
Family (HMM) version: 5
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Species distribution

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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 ecTbetaR2 domain has been found. There are 9 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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