Binding to phosphatidyl serine membranes causes a conformational change in the concave face of annexin I
Author
dc.contributor.author
Fuente, Milton de la
Author
dc.contributor.author
Ossa, Carmen Gloria
Admission date
dc.date.accessioned
2019-01-29T15:55:07Z
Available date
dc.date.available
2019-01-29T15:55:07Z
Publication date
dc.date.issued
1997
Cita de ítem
dc.identifier.citation
Biophysical Journal Volume 71 January 1997 383-387
Identifier
dc.identifier.issn
00063495
Identifier
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10.1016/S0006-3495(97)78677-6
Identifier
dc.identifier.uri
https://repositorio.uchile.cl/handle/2250/162787
Abstract
dc.description.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.