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Domain binding and function: Domain binding and function: Leucine-Rich Repeats (LRR) are 22À28 amino acid motifs that are found in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in proteinÀprotein interactions, and in series they form nonglobular, crescent-shaped structures. The crescent shape adopted by series of leucine-rich repeats creates a solventexposed elongated concave surface of parallel beta-strands that acts as a scaffold for proteinÀprotein 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. Structure Reference: Hillig, R.C. et al. (1999) Mol. Cell 3(6), 781À791. Examples of Domain Proteins: |
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Binding Examples:
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FHA domain proteins |  |
Binding partners |  |
| RNAse Inhibitor | RNAse | |||
| Rna1p | RAN small GTPase | |||
| TAP | Constitutive transport element (CTE) of retroviral RNAs | |||
| U2A' | Ribonucleoprotein domain of U2B' | |||
| CIITA | MHC class II promoter binding complex |
