4.7 Review

The leucine-rich repeat structure

Journal

CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 65, Issue 15, Pages 2307-2333

Publisher

SPRINGER BASEL AG
DOI: 10.1007/s00018-008-8019-0

Keywords

leucine-rich repeat; protein structure; protein conformation; protein-protein interactions; molecular sequence data; molecular models; protein engineering; repetitive sequences

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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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