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.
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Received 11 January 2008; received after revision 7 March 2008; accepted 10 March 2008
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Bella, J., Hindle, K.L., McEwan, P.A. et al. The leucine-rich repeat structure. Cell. Mol. Life Sci. 65, 2307–2333 (2008). https://doi.org/10.1007/s00018-008-8019-0
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DOI: https://doi.org/10.1007/s00018-008-8019-0