Summary: Vitamin D binding protein, domain III
This is the Wikipedia entry entitled "Vitamin D binding protein domain III". More...
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Vitamin D binding protein domain III Edit Wikipedia article
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crystal structure of uncomplexed vitamin d-binding protein
In molecular biology, Vitamin D binding protein domain III protein domain is predominantly found in Vitamin D binding proteins (DBP). Vitamin D-binding protein (DBP)(also referred to as Gc-globulin) is synthesized primarily in the liver. This entry outlines the domain III of DBP. Domain III (amino acid 379–458) is G-actin binding region located in the C-terminal. Domain (amino acids 373 to 403). This protein is found ubiquitously in vivo in significant quantities and can be detected in all fluid compartments. During acute phase inflammatory respose, DBP levels tend to increase.
DBP domain III has a multihelical structure. It is required for formation of an actin 'clamp', allowing the protein to bind to actin. This protein is a member of the albumin gene family and has the characteristic multiple disulfide-bonded, triple domain structure.
- Zhang J, Habiel DM, Ramadass M, Kew RR (2010). "Identification of two distinct cell binding sequences in the vitamin D binding protein.". Biochim Biophys Acta 1803 (5): 623–9. doi:10.1016/j.bbamcr.2010.02.010. PMC 2856814. PMID 20211661.
- Otterbein LR, Cosio C, Graceffa P, Dominguez R (June 2002). "Crystal structures of the vitamin D-binding protein and its complex with actin: structural basis of the actin-scavenger system". Proc. Natl. Acad. Sci. U.S.A. 99 (12): 8003–8. doi:10.1073/pnas.122126299. PMC 123010. PMID 12048248.
Vitamin D binding protein, domain III Provide feedback
Members of this family are predominantly found in Vitamin D binding protein, and adopt a multihelical structure. They are required for formation of an actin 'clamp', allowing the protein to bind to actin .
Otterbein LR, Cosio C, Graceffa P, Dominguez R; , Proc Natl Acad Sci U S A. 2002;99:8003-8008.: Crystal structures of the vitamin D-binding protein and its complex with actin: structural basis of the actin-scavenger system. PUBMED:12048248 EPMC:12048248
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR015247
This domain is predominantly found in Vitamin D binding proteins, and adopts a multihelical structure. It is required for formation of an actin 'clamp', allowing the protein to bind to actin [PUBMED:12048248].
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This example describes an architecture with one
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EGFdomains, and finally a single
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We make a range of alignments for each Pfam-A family:
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Curation and family details
|Number in seed:||6|
|Number in full:||46|
|Average length of the domain:||67.30 aa|
|Average identity of full alignment:||58 %|
|Average coverage of the sequence by the domain:||14.43 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||5|
|Download:||download the raw HMM for this family|
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There are 3 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 VitD-bind_III 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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