Kobe B, Deisenhofer J
Howard Hughes Medical Institute, Dallas, TX.
Trends Biochem Sci. 1994 Oct;19(10):415-21. doi: 10.1016/0968-0004(94)90090-6.
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.
富含亮氨酸的重复序列是存在于许多具有不同功能和细胞定位的蛋白质中的短序列基序。所有含有这些重复序列的蛋白质都被认为参与蛋白质-蛋白质相互作用。核糖核酸酶抑制蛋白的晶体结构表明,富含亮氨酸的重复序列对应于β-α结构单元。这些单元排列成平行的β-折叠,其中一个表面暴露于溶剂中,从而使该蛋白质获得一种不寻常的、非球状的形状。这两个特征可能是含有富含亮氨酸重复序列的蛋白质具有蛋白质结合功能的原因。