TY - JOUR
T1 - The leucine-rich repeat
T2 - a versatile binding motif
AU - Kobe, Bostjan
AU - Deisenhofer, Johann
N1 - Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1994/10
Y1 - 1994/10
N2 - 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 β-α structural units. These units are arranged so that they form a parallel β-sheet with one surface exposed to solvent, so that the protein acquires an unusual, non-globular shape. These two features may be responsible for the protein-binding functions of proteins containing leucine-rich repeats.
AB - 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 β-α structural units. These units are arranged so that they form a parallel β-sheet with one surface exposed to solvent, so that the protein acquires an unusual, non-globular shape. These two features may be responsible for the protein-binding functions of proteins containing leucine-rich repeats.
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U2 - 10.1016/0968-0004(94)90090-6
DO - 10.1016/0968-0004(94)90090-6
M3 - Review article
C2 - 7817399
AN - SCOPUS:0028080261
SN - 0968-0004
VL - 19
SP - 415
EP - 421
JO - Trends in biochemical sciences
JF - Trends in biochemical sciences
IS - 10
ER -