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Leucine-rich-repeat (LRR) proteins are characterized by repeats of 26-29 residues that adopt a regular solenoid of α-helices (on the outside) and β-strands (on the inside). The solenoid can curve into a simple arc (as for ribonuclease inhibitor), but usually twists into a segment of a helix (as for YopM from Yersinia pestis). LRR domains are often used for forming protein-protein interactions.
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