The leucine-rich repeat as a protein recognition motif
The leucine-rich repeat as a protein recognition motif
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DOI：
10.1016/s0959-440x(01)00266-4
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发表时间：
2001-12-01
影响因子：
6.8
通讯作者：
Kajava, AV
中科院分区：
文献类型：
--
作者：
Kobe, B;Kajava, AV
富亮氨酸重复序列(LRR)是存在于多种蛋白质中的20-29个残基的序列模体，具有不同的功能。这些基序的主要功能似乎是为蛋白质-蛋白质相互作用的形成提供一个多功能的结构框架。在过去的两年里，使用LRRS看到了关于蛋白质的新的结构信息的爆炸性增长。这些新结构代表了不同的LRR亚家族和具有不同功能的蛋白质，包括来自核糖核酸酶抑制物亚家族的GTP酶激活蛋白RNA1p；来自SDS22类似亚家族的剪接体蛋白U2a‘、Rab geranylgeranyl转移酶、内源性B、动力蛋白轻链1和核输出蛋白TAP；来自含半胱氨酸的亚家族的Skp2；来自细菌亚家族的YopM。新的结构信息增加了我们对LRR蛋白质结构决定因素的理解，以及我们对具有未知结构的蛋白质建模的能力，并为这些蛋白质如何参与蛋白质-蛋白质相互作用提供了新的线索。
Leucine-rich repeats (LRRs) are 20-29-residue sequence motifs present in a number of proteins with diverse functions. The primary function of these motifs appears to be to provide a versatile structural framework for the formation of protein-protein interactions. The past two years have seen an explosion of new structural information on proteins with LRRs. The new structures represent different LRR subfamilies and proteins with diverse functions, including GTPase-activating protein rna 1 p from the ribonuclease-inhibitor-like subfamily; spliceosomal protein U2A', Rab geranylgeranyltransferase, internalin B, dynein light chain 1 and nuclear export protein TAP from the SDS22-like subfamily; Skp2 from the cysteine-containing subfamily; and YopM from the bacterial subfamily. The new structural information has increased our understanding of the structural determinants of LRR proteins and our ability to model such proteins with unknown structures, and has shed new light on how these proteins participate in protein-protein interactions.