Ernst J D
Department of Medicine, University of California, San Francisco.
Biochem J. 1993 Jan 15;289 ( Pt 2)(Pt 2):539-42. doi: 10.1042/bj2890539.
To understand further the structural basis of phospholipid binding by annexin I, three monoclonal antibodies that compete with Ca2+ and phospholipids for binding of annexin I were used to screen an expression library containing fragments of bovine annexin I cDNA. In all, 15 clones were isolated, and all contain overlapping fragments of the cDNA. The smallest unit common to all of the clones encodes amino acids 42-99 of annexin I, representing a portion of the first repeat domain. This demonstrates that recognition of a single domain of annexin I is sufficient to completely block phospholipid binding, and implies that the first repeat may contribute to phospholipid binding by annexin I.
为了进一步了解膜联蛋白I结合磷脂的结构基础,使用三种与Ca2+和磷脂竞争结合膜联蛋白I的单克隆抗体来筛选一个包含牛膜联蛋白I cDNA片段的表达文库。总共分离出15个克隆,所有克隆都包含cDNA的重叠片段。所有克隆共有的最小单位编码膜联蛋白I的42 - 99位氨基酸,代表第一个重复结构域的一部分。这表明识别膜联蛋白I的单个结构域足以完全阻断磷脂结合,并暗示第一个重复结构可能有助于膜联蛋白I与磷脂的结合。