The leucine-rich repeat: a versatile binding motif

Bostjan Kobe, Johann Deisenhofer

Research output: Contribution to journalArticle

966 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)415-421
Number of pages7
JournalTrends in Biochemical Sciences
Volume19
Issue number10
DOIs
StatePublished - 1994

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Leucine
Proteins
Ribonucleases
Protein Binding
Carrier Proteins
Crystal structure

ASJC Scopus subject areas

  • Biochemistry

Cite this

The leucine-rich repeat : a versatile binding motif. / Kobe, Bostjan; Deisenhofer, Johann.

In: Trends in Biochemical Sciences, Vol. 19, No. 10, 1994, p. 415-421.

Research output: Contribution to journalArticle

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