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

Bostjan Kobe, Johann Deisenhofer

Research output: Contribution to journalArticle

544 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)183-186
Number of pages4
JournalNature
Volume374
Issue number6518
StatePublished - 1995

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Leucine
Ligands
Pancreatic Ribonuclease
Amino Acid Motifs
Ribonucleases
Protein Binding
Cell Adhesion
DNA Repair
Signal Transduction
RNA
Proteins
leucine-rich repeat proteins

ASJC Scopus subject areas

  • General

Cite this

A structural basis of the interactions between leucine-rich repeats and protein ligands. / Kobe, Bostjan; Deisenhofer, Johann.

In: Nature, Vol. 374, No. 6518, 1995, p. 183-186.

Research output: Contribution to journalArticle

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