Binding to phosphatidyl serine membranes causes a conformational change in the concave face of annexin I
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1997Metadata
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Binding to phosphatidyl serine membranes causes a conformational change in the concave face of annexin I
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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 Ca2+-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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URI: https://repositorio.uchile.cl/handle/2250/162787
DOI: 10.1016/S0006-3495(97)78677-6
ISSN: 00063495
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Biophysical Journal Volume 71 January 1997 383-387
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