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- W2004152842 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." @default.
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- W2004152842 date "1993-09-03" @default.
- W2004152842 modified "2023-10-11" @default.
- W2004152842 title "Rat Annexin V Crystal Structure: Ca<sup>2+</sup>-Induced Conformational Changes" @default.
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- W2004152842 doi "https://doi.org/10.1126/science.8362244" @default.
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