Biophysical Journal 72: 383-387 (1997)
© 1997 the Biophysical Society

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

Departamento de Fislología y Biofísica, Facultad de Medicina, Universidad de Chile, Santiago, Chile. mdelafue@machi.med.uchile.cl

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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