Structural highlights
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
