The leucine-rich repeat as a protein recognition motif

Kobe, Bostjan and Kajava, Andrey V. (2001) The leucine-rich repeat as a protein recognition motif. Current Opinion In Structural Biology, 11 6: 725-732. doi:10.1016/S0959-440X(01)00266-4

Author Kobe, Bostjan
Kajava, Andrey V.
Title The leucine-rich repeat as a protein recognition motif
Journal name Current Opinion In Structural Biology   Check publisher's open access policy
ISSN 0959-440X
Publication date 2001-12-01
Year available 2001
Sub-type Article (original research)
DOI 10.1016/S0959-440X(01)00266-4
Open Access Status Not yet assessed
Volume 11
Issue 6
Start page 725
End page 732
Total pages 8
Place of publication London
Publisher Elsevier Science Ltd.
Language eng
Subject C1
270100 Biochemistry and Cell Biology
780105 Biological sciences
Abstract Leucine-rich repeats (LRRs) are 20-29-residue sequence motifs present in a number of proteins with diverse functions. The primary function of these motifs appears to be to provide a versatile structural framework for the formation of protein-protein interactions. The past two years have seen an explosion of new structural information on proteins with LRRs. The new structures represent different LRR subfamilies and proteins with diverse functions, including GTPase-activating protein rna 1 p from the ribonuclease-inhibitor-like subfamily; spliceosomal protein U2A', Rab geranylgeranyltransferase, internalin B, dynein light chain 1 and nuclear export protein TAP from the SDS22-like subfamily; Skp2 from the cysteine-containing subfamily; and YopM from the bacterial subfamily. The new structural information has increased our understanding of the structural determinants of LRR proteins and our ability to model such proteins with unknown structures, and has shed new light on how these proteins participate in protein-protein interactions.
Keyword Biochemistry & Molecular Biology
Cell Biology
Porcine Ribonuclease Inhibitor
2.0 Angstrom Resolution
Q-Index Code C1
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
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Created: Wed, 15 Aug 2007, 01:17:24 EST