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蛋白质-蛋白质相互作用对细胞内囊泡运输特异性的作用。

Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking.

作者信息

Calakos N, Bennett M K, Peterson K E, Scheller R H

机构信息

Howard Hughes Medical Institute, Stanford University Medical Center, CA 94305.

出版信息

Science. 1994 Feb 25;263(5150):1146-9. doi: 10.1126/science.8108733.

Abstract

Intracellular vesicles destined to fuse with the plasma membrane and secrete their contents must have a mechanism for specifically interacting with the appropriate target membrane. Such a mechanism is now suggested by the demonstration of specific interaction between vesicular proteins and plasma membrane proteins. The vesicle-associated membrane proteins (VAMPs) 1 and 2 specifically bind the acceptor membrane proteins syntaxin 1A and 4 but not syntaxin 2 or 3. The binding site is within amino acids 194 to 267 of syntaxin 1A, and the approximate equilibrium dissociation constants is 4.7 x 10(-6) molar. These data suggest a physical basis for the specificity of intracellular vesicular transport.

摘要

注定要与质膜融合并分泌其内容物的细胞内囊泡必须有一种机制,用于与合适的靶膜进行特异性相互作用。囊泡蛋白与质膜蛋白之间特异性相互作用的证明,为这种机制提供了线索。囊泡相关膜蛋白(VAMPs)1和2特异性结合受体膜蛋白 syntaxin 1A和4,而不与syntaxin 2或3结合。结合位点在syntaxin 1A的第194至267个氨基酸内,近似平衡解离常数为4.7×10⁻⁶摩尔。这些数据为细胞内囊泡运输的特异性提供了物理基础。

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