Rat annexin V crystal structure: Ca(2+)-induced conformational changes.
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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Department of Physiology, Boston University School of Medicine, MA 02118.
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J F
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Kaetzel
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Dedman
J R
JR
Seaton
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D000595:Amino Acid Sequence; D000818:Animals; D017304:Annexin A5 / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism*; D003196:Computer Graphics; D003460:Crystallization; D006801:Humans; D006860:Hydrogen Bonding; D008969:Molecular Sequence Data; D011487:Protein Conformation; D051381:Rats; D016415:Sequence Alignment; D014364:Tryptophan / Q000737:chemistry; D014961:X-Ray Diffraction
D017304:Annexin A5; D014364:Tryptophan; D002118:Calcium