The leucine-rich repeat: a versatile binding motif.

Abstract

Leucine-rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. All proteins containing these repeats are thought to be involved in protein-protein interactions. The crystal structure of ribonuclease inhibitor protein has revealed that leucine-rich repeats correspond to beta-alpha structural units. These units are arranged so that they form a parallel beta-sheet with one surface exposed to solvent, so that the protein acquires an unusual, nonglobular shape. These two features may be responsible for the protein-binding functions of proteins containing leucine-rich repeats.

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@article{Kobe1994TheLR, title={The leucine-rich repeat: a versatile binding motif.}, author={Bostjan Kobe and Johann Deisenhofer}, journal={Trends in biochemical sciences}, year={1994}, volume={19 10}, pages={415-21} }