IPR000483
Cysteine-rich flanking region, C-terminal
InterPro entry
Short name | Cys-rich_flank_reg_C |
Overlapping homologous superfamilies | |
domain relationships |
Description
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
[1]. LRRs occur in proteins ranging from viruses to eukaryotes, and appear to provide a structural framework for the formation of protein-protein interactions
[2]. 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.
References
1.Structural principles of leucine-rich repeat (LRR) proteins. Enkhbayar P, Kamiya M, Osaki M, Matsumoto T, Matsushima N. Proteins 54, 394-403, (2004). View articlePMID: 14747988
2.The leucine-rich repeat as a protein recognition motif. Kobe B, Kajava AV. Curr. Opin. Struct. Biol. 11, 725-32, (2001). View articlePMID: 11751054