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Leucine-rich repeat

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Gene Music using Protein Sequence of LRRC25 "LEUCINE RICH REPEAT CONTAINING 25"

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Gene Music using Protein Sequence of LRRC37B "LEUCINE RICH REPEAT CONTAINING 37B"

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Gene Music using Protein Sequence of LRRC59 "LEUCINE RICH REPEAT CONTAINING 59"

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Gene Music using Protein Sequence of LRRC36 "LEUCINE RICH REPEAT CONTAINING 36"

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Gene Music using Protein Sequence of LRSAM1 "LEUCINE RICH REPEAT AND STERILE ALPHA MOTIF CONTAINING"

A leucine-rich repeat (LRR) is a protein structural motif that forms an α/β horseshoe fold. It is composed of repeating 20–30 amino acid stretches that are unusually rich in the hydrophobic amino acid leucine. These repeats commonly fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Typically, each repeat unit has beta strand-turn-alpha helix structure, and the assembled domain, composed of many such repeats, has a horseshoe shape with an interior parallel beta sheet and an exterior array of helices. One face of the beta sheet and one side of the helix array are exposed to solvent and are therefore dominated by hydrophilic residues. The region between the helices and sheets is the protein's hydrophobic core and is tightly sterically packed with leucine residues.
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