Biology:Vitamin D binding protein domain III
| VitD-bind_III | |||||||||
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 crystal structure of uncomplexed vitamin d-binding protein | |||||||||
| Identifiers | |||||||||
| Symbol | VitD-bind_III | ||||||||
| Pfam | PF09164 | ||||||||
| Pfam clan | CL0282 | ||||||||
| InterPro | IPR015247 | ||||||||
| SCOP2 | 1kxp / SCOPe / SUPFAM | ||||||||
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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.
Function
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
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
- ↑ 1.0 1.1 "Identification of two distinct cell binding sequences in the vitamin D binding protein.". Biochim Biophys Acta 1803 (5): 623–9. 2010. doi:10.1016/j.bbamcr.2010.02.010. PMID 20211661.
- ↑ "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. June 2002. doi:10.1073/pnas.122126299. PMID 12048248. Bibcode: 2002PNAS...99.8003O.
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