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Science 3 September 1993:
Vol. 261. no. 5126, pp. 1321 - 1324
DOI: 10.1126/science.8362244
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Articles

Science, Vol 261, Issue 5126, 1321-1324
Copyright © 1993 by American Association for the Advancement of Science

articles

Rat annexin V crystal structure: Ca(2+)-induced conformational changes

NO Concha, JF Head, MA Kaetzel, Dedman JR, and BA Seaton

Department of Physiology, Boston University School of Medicine, MA 02118.

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.


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