Vitamin D binding protein domain III
| 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 | ||||||||
| |||||||||
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[edit]
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[edit]
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[edit]
- ^ 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.
- ^ 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.