A STRUCTURAL BASIS OF THE INTERACTIONS BETWEEN LEUCINE-RICH REPEATS AND PROTEIN LIGANDS
A STRUCTURAL BASIS OF THE INTERACTIONS BETWEEN LEUCINE-RICH REPEATS AND PROTEIN LIGANDS
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DOI：
10.1038/374183a0
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发表时间：
1995-03-09
期刊：
影响因子：
64.8
通讯作者：
DEISENHOFER, J
中科院分区：
文献类型：
--
作者：
KOBE, B;DEISENHOFER, J
富含亮氨酸的重复序列是最近表征的结构基序（1），用于多种分子识别过程，如信号转导、细胞粘附、细胞发育、DNA修复和RNA加工（2）。我们在这里提出了核糖核酸酶A和核糖核酸酶抑制剂之间的复合物在2.5埃分辨率的晶体结构，一种完全由富含亮氨酸的重复序列构建的蛋白质，核糖核酸酶抑制剂的不寻常的非球形结构，其溶剂暴露的平行β-折叠和结构的构象灵活性被用于相互作用;它们似乎是富含亮氨酸的重复序列作为蛋白质结合基序的有效性的主要原因。该结构可以作为含有富含亮氨酸的重复序列的其他蛋白质与其配体相互作用的模型。
THE leucine-rich repeat is a recently characterized structural motif(1) used in molecular recognition processes as diverse as signal transduction, cell adhesion, cell development, DNA repair and RNA processing(2). We present here the crystal structure at 2.5 Angstrom resolution of the complex between ribonuclease A and ribonculease inhibitor, a protein built entirely of leucine-rich repeats, The unusual non-globular structure of ribonuclease inhibitor, its solvent-exposed parallel beta-sheet and the conformational flexibility of the structure are used in the interaction; they appear to be the principal reasons for the effectiveness of leucine-rich repeats as protein-binding motifs, The structure can serve as a model for the interactions of other proteins containing leucine-rich repeats with their ligands.