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

Nature volume 374, pages 183–186 (1995)Cite this article

Abstract

THE leucine-rich repeat is a recently characterized structural motif1 used in molecular recognition processes as diverse as signal transduction, cell adhesion, cell development, DNA repair and RNA processing2. 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 β-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.

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Author notes

  1. Bostjan Kobe

    Present address: St Vincent's Institute of Medical Research, 41 Victoria Parade, Fitzroy, Victoria, 3065, Australia

Authors and Affiliations

  1. Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas, 75235-9050, USA

    Bostjan Kobe & Johann Deisenhofer

  2. on leave from Jozef Stefan Institute, Department of Biochemistry and Molecular Biology, Jamova 39, 61111, Ljubljana, Slovenia

    Bostjan Kobe

Authors
  1. Bostjan Kobe
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  2. Johann Deisenhofer
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Kobe, B., Deisenhofer, J. A structural basis of the interactions between leucine-rich repeats and protein ligands. Nature 374, 183–186 (1995). https://doi.org/10.1038/374183a0

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  • DOI: https://doi.org/10.1038/374183a0

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