Referenced in: none

Automatically associated channels: Kir2.3

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

Authors: N O Concha, J F Head, M A Kaetzel, J R Dedman, B A Seaton

Journal, date & volume: Science, 1993 Sep 3 , 261, 1321-4

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/8362244

Abstract
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.