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Article

Interfacial basic cluster in annexin V couples phospholipid binding and trimer formation on membrane surfaces.

The Journal of biological chemistry - 24 Jan 2003

Mo Youde, Campos Begoña, Mealy Tanya R, Commodore Lois, Head James F, Dedman John R, Seaton Barbara A

Abstract excerpt

Annexin V is an abundant eukaryotic protein that binds phospholipid membranes in a Ca(2+)-dependent manner. In the present studies, site-directed mutagenesis was combined with x-ray crystallography and solution liposome binding assays to probe the functional role of a cluster of interfacial basic residues in annexin V. Four mutants were investigated: R23E, K27E, R61E, and R149E. All four mutants exhibited a...

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Identifiers

PMID: 12401794
DOI: 10.1074/jbc.M210286200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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