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. 1997 Jan;72(1):383–387. doi: 10.1016/S0006-3495(97)78677-6

Binding to phosphatidyl serine membranes causes a conformational change in the concave face of annexin I.

M de la Fuente 1, C G Ossa 1
PMCID: PMC1184327  PMID: 8994623

Abstract

Recent studies have revealed that binding of annexin I to phospholipids induces the formation of a second phospholipid binding site. It is shown that the N terminus on the concave side of membrane-bound annexin I is cleaved much faster by trypsin or cathepsin than the N terminus of the free protein. The reactivity of the unique disulfide bond located near the concave face was similarly increased by membrane binding. These results demonstrate that Ca(2+)-dependent membrane binding induces a conformational change on the concave side of the annexin I molecule and support the notion that this face of the molecule may contribute to the formation of the secondary membrane-binding site.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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