The leucine-rich repeat: a versatile binding motif

Trends Biochem Sci. 1994 Oct;19(10):415-21. doi: 10.1016/0968-0004(94)90090-6.


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 beta-alpha structural units. These units are arranged so that they form a parallel beta-sheet with one surface exposed to solvent, so that the protein acquires an unusual, nonglobular shape. These two features may be responsible for the protein-binding functions of proteins containing leucine-rich repeats.

Publication types

  • Review

MeSH terms

  • Animals
  • Binding Sites
  • Biological Evolution
  • Consensus Sequence
  • Humans
  • Leucine*
  • Protein Structure, Secondary
  • Proteins / chemistry*
  • Repetitive Sequences, Nucleic Acid*
  • Signal Transduction


  • Proteins
  • Leucine