THE LEUCINE-RICH REPEAT - A VERSATILE BINDING MOTIF

被引：1057

作者：

KOBE, B ^{[1
]}

DEISENHOFER, J ^{[1
]}

机构：

[1] UNIV TEXAS,SW MED CTR,DEPT BIOCHEM,DALLAS,TX 75235

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 1994年 / 19卷 / 10期

关键词：

D O I：

10.1016/0968-0004(94)90090-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Leucine-rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. All proteins containing these repeats are thought to be involved in protein-protein interactions. The crystal structure of ribonuclease inhibitor protein has revealed that leucine-rich repeats correspond to beta-alpha structural units. These units are arranged so that they form a parallel beta-sheet with one surface exposed to solvent, so that the protein acquires an unusual, nonglobular shape. These two features may be responsible for the protein-binding functions of proteins containing leucine-rich repeats.

引用

页码：415 / 421

页数：7

共 42 条

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