Vitamin D binding protein domain III

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.[1] During acute phase inflammatory response, DBP levels tend to increase.

VitD-bind_III
crystal structure of uncomplexed vitamin d-binding protein
crystal structure of uncomplexed vitamin d-binding protein
Identifiers
SymbolVitD-bind_III
PfamPF09164
Pfam clanCL0282
InterProIPR015247
SCOP21kxp / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Function

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DBP has several functions. More precisely, domain III has the specific function of being an extracellular scavenger for G-actin released from necrotic cells at sites of tissue injury.[1]

Structure

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DBP domain III has a multihelical structure. It is required for formation of an actin 'clamp', allowing the protein to bind to actin.[2] This protein is a member of the albumin gene family and has the characteristic multiple disulfide-bonded, triple domain structure.

References

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  1. ^ a b 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.
  2. ^ 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. Bibcode:2002PNAS...99.8003O. doi:10.1073/pnas.122126299. PMC 123010. PMID 12048248.
This article incorporates text from the public domain Pfam and InterPro: IPR015247