The leucine-rich repeat structure

被引:0
|
作者
J. Bella
K. L. Hindle
P. A. McEwan
S. C. Lovell
机构
[1] University of Manchester,Wellcome Trust Centre for Cell
[2] University of Nottingham,Matrix Research, Faculty of Life Sciences
[3] University Park,School of Pharmacy, Centre for Biomolecular Sciences
来源
Cellular and Molecular Life Sciences | 2008年 / 65卷
关键词
Leucine-rich repeat; protein structure; protein conformation; protein-protein interactions; molecular sequence data; molecular models; protein engineering; repetitive sequences;
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学科分类号
摘要
The leucine-rich repeat is a widespread structural motif of 20–30 amino acids with a characteristic repetitive sequence pattern rich in leucines. Leucine-rich repeat domains are built from tandems of two or more repeats and form curved solenoid structures that are particularly suitable for protein-protein interactions. Thousands of protein sequences containing leucine-rich repeats have been identified by automatic annotation methods. Three-dimensional structures of leucine-rich repeat domains determined to date reveal a degree of structural variability that translates into the considerable functional versatility of this protein superfamily. As the essential structural principles become well established, the leucine-rich repeat architecture is emerging as an attractive framework for structural prediction and protein engineering. This review presents an update of the current understanding of leucine-rich repeat structure at the primary, secondary, tertiary and quaternary levels and discusses specific examples from recently determined three-dimensional structures.
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页码:2307 / 2333
页数:26
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