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• W2073764175 startingPage "415" @default.
• W2073764175 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." @default.
• W2073764175 created "2016-06-24" @default.
• W2073764175 creator A5033642634 @default.
• W2073764175 creator A5053221368 @default.
• W2073764175 date "1994-10-01" @default.
• W2073764175 modified "2023-10-03" @default.
• W2073764175 title "The leucine-rich repeat: a versatile binding motif" @default.
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• W2073764175 doi "https://doi.org/10.1016/0968-0004(94)90090-6" @default.
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