Leucine-rich repeats (LRR, see IPR001611 ) consist of 2-45 motifs of 20-30 amino acids in length that generally folds into an arc or horseshoe shape [ PUBMED:14747988 ]. LRRs occur in proteins ranging from viruses to eukaryotes, and … expand

Leucine-rich repeats (LRR, see IPR001611 ) consist of 2-45 motifs of 20-30 amino acids in length that generally folds into an arc or horseshoe shape [ PUBMED:14747988 ]. LRRs occur in proteins ranging from viruses to eukaryotes, and appear to provide a structural framework for the formation of protein-protein interactions [ PUBMED:11751054 ]. Proteins containing LRRs include tyrosine kinase receptors, cell-adhesion molecules, virulence factors, and extracellular matrix-binding glycoproteins, and are involved in a variety of biological processes, including signal transduction, cell adhesion, DNA repair, recombination, transcription, RNA processing, disease resistance, apoptosis, and the immune response.

LRRs are often flanked by cysteine-rich domains: an N-terminal LRR domain ( IPR000372 ) and a C-terminal LRR domain. This entry represents the C-terminal LRR domain.