Structural highlights
Function
[ANXA5_RAT] This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Annexins are a family of calcium- and phospholipid-binding proteins implicated in mediating membrane-related processes such as secretion, signal transduction, and ion channel activity. The crystal structure of rat annexin V was solved to 1.9 angstrom resolution by multiple isomorphous replacement. Unlike previously solved annexin V structures, all four domains bound calcium in this structure. Calcium binding in the third domain induced a large relocation of the calcium-binding loop regions, exposing the single tryptophan residue to the solvent. These alterations in annexin V suggest a role for domain 3 in calcium-triggered interaction with phospholipid membranes.
Rat annexin V crystal structure: Ca(2+)-induced conformational changes.,Concha NO, Head JF, Kaetzel MA, Dedman JR, Seaton BA Science. 1993 Sep 3;261(5126):1321-4. PMID:8362244[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Concha NO, Head JF, Kaetzel MA, Dedman JR, Seaton BA. Rat annexin V crystal structure: Ca(2+)-induced conformational changes. Science. 1993 Sep 3;261(5126):1321-4. PMID:8362244
