2ran
From Proteopedia
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[[Image:2ran.jpg|left|200px]] | [[Image:2ran.jpg|left|200px]] | ||
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'''RAT ANNEXIN V CRYSTAL STRUCTURE: CA2+-INDUCED CONFORMATIONAL CHANGES''' | '''RAT ANNEXIN V CRYSTAL STRUCTURE: CA2+-INDUCED CONFORMATIONAL CHANGES''' | ||
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[[Category: Kaetzel, M A.]] | [[Category: Kaetzel, M A.]] | ||
[[Category: Seaton, B A.]] | [[Category: Seaton, B A.]] | ||
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Revision as of 13:33, 4 May 2008
RAT ANNEXIN V CRYSTAL STRUCTURE: CA2+-INDUCED CONFORMATIONAL CHANGES
Overview
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.
About this Structure
2RAN is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sun May 4 16:33:31 2008