2ran
From Proteopedia
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| , resolution 1.89Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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