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Cellular and Molecular Life Sciences: CMLS logoLink to Cellular and Molecular Life Sciences: CMLS
. 2008 Apr 14;65(15):2307–2333. doi: 10.1007/s00018-008-8019-0

The leucine-rich repeat structure

J Bella 1,, K L Hindle 1, P A McEwan 2, S C Lovell 1
PMCID: PMC11131621  PMID: 18408889

Abstract.

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.

Keywords. Leucine-rich repeat, protein structure, protein conformation, protein-protein interactions, molecular sequence data, molecular models, protein engineering, repetitive sequences

Footnotes

Received 11 January 2008; received after revision 7 March 2008; accepted 10 March 2008


Articles from Cellular and Molecular Life Sciences: CMLS are provided here courtesy of Springer

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