de la Fuente M, Ossa C G
Departamento de Fislología y Biofísica, Facultad de Medicina, Universidad de Chile, Santiago, Chile.
Biophys J. 1997 Jan;72(1):383-7. doi: 10.1016/S0006-3495(97)78677-6.
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.
最近的研究表明，膜联蛋白I与磷脂结合会诱导形成第二个磷脂结合位点。结果显示，膜结合型膜联蛋白I凹面的N端被胰蛋白酶或组织蛋白酶切割的速度比游离蛋白的N端快得多。位于凹面附近的独特二硫键的反应性同样因膜结合而增加。这些结果表明，Ca(2+)依赖的膜结合会诱导膜联蛋白I分子凹面发生构象变化，并支持该分子的这一面可能有助于形成二级膜结合位点这一观点。
