 LRR Domain | |
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Structure:
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Domain binding and function:
 Domain binding and function: Leucine-Rich Repeats (LRR) are 22-28 amino acid motifs that are found in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions, and in series they form nonglobular, crescent-shaped structures. The crescent shape adopted by series of leucine-rich repeats creates a solvent-exposed elongated concave surface of parallel beta-strands that acts as a scaffold for protein-protein interactions. The particular function of each LRR crescent is specified by different residues arranged in an appropriate orientation on the surface of the structurally conserved three-dimensional fold. For example, RNAse inhibitor and U2A' LRR scaffolds appear to interact with their targets via the concave inner surface of the crescent, while in the case of S. pombe Rna1p, the Ran binding site appears to be located on the side face of the crescent within the loop regions connecting the beta-strands and alpha-helices.
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Examples of Proteins:
| LRR domain proteins |
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Binding partners |
| RNAse Inhibitor |  |
RNAse |
| Rna1p | |
RAN small GTPase |
| TAP | |
Constitutive transport element of retroviral RNAs |
| U2A' | |
Ribonucleoprotein domain of U2B' |
| CIITA | |
MHC class II promoter binding complex |
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Referenced in part on Cell Signaling Technology Website, Reference Section on Protein Domains. We gratefully acknowledge the following contributors:
Piers Nash1, Dan Lin3, Kathleen Binns2, Clark Wells2, Rob Ingham2, Terry Kubiseski2, Bernard Liu1, Matt Smith2,3, Ivan Blasutig2,3, Maria Sierra1, Caesar Lim2,3, Michael Arc1, Jim Fawcett2 and Tony Pawson2,3.
1. Ben May Institute for Cancer Research, The University of Chicago, Chicago, Illinois, 60637, USA
2. Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, M5G 1X5, Canada
3. Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario, M5S 1A8, Canada
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