A structural basis of the interactions between leucine-rich repeats and protein ligands

Kobe, Bostjan and Deisenhofer, Johann (1995) A structural basis of the interactions between leucine-rich repeats and protein ligands. Nature, 374 6518: 183-186. doi:10.1038/374183a0


Author Kobe, Bostjan
Deisenhofer, Johann
Title A structural basis of the interactions between leucine-rich repeats and protein ligands
Journal name Nature   Check publisher's open access policy
ISSN 0028-0836
1476-4687
Publication date 1995-01-01
Sub-type Article (original research)
DOI 10.1038/374183a0
Volume 374
Issue 6518
Start page 183
End page 186
Total pages 4
Place of publication London, UK
Publisher Nature Publishing Group
Language eng
Subject 060112 Structural Biology (incl. Macromolecular Modelling)
Formatted abstract
THE leucine-rich repeat is a recently characterized structural motif used in molecular recognition processes as diverse as signal transduction, cell adhesion, cell development, DNA repair and RNA processing. We present here the crystal structure at 2.5 Å resolution of the complex between ribonuclease A and ribonculease inhibitor, a protein built entirely of leucine-rich repeats. The unusual non-globular structure of ribonuclease inhibitor, its solvent-exposed parallel ß-sheet and the conformational flexibility of the structure are used in the interaction; they appear to be the principal reasons for the effectiveness of leucine-rich repeats as protein-binding motifs. The structure can serve as a model for the interactions of other proteins containing leucine-rich repeats with their ligands.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
 
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Created: Wed, 21 Jul 2010, 00:29:53 EST by Laura McTaggart on behalf of Faculty of Science