| VitD-bind_III | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 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. 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.
Structure
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.
References
- ^ 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. Bibcode:2002PNAS...99.8003O. doi:10.1073/pnas.122126299. PMC 123010. PMID 12048248.