title: 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.
authors: Howard Hughes Medical Institute, Dallas, TX.
authors: B
authors: B
authors: Kobe
authors: J
authors: J
authors: Deisenhofer
mesh_terms: D000818:Animals; D001665:Binding Sites; D005075:Biological Evolution; D016384:Consensus Sequence; D006801:Humans; D007930:Leucine; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D012091:Repetitive Sequences, Nucleic Acid; D015398:Signal Transduction
chemical_list: D011506:Proteins; D007930:Leucine