logo

Video encyclopedia

Leucine-rich repeat

35:21

Leucine rich repeat kinase 2: From pathology to physiology and back // Patrick Lewis

1:51

International Academy of Cardiology: Randolph Hutter, M.D.: THE NOVEL SMALL LEUCINE RICH-REPEAT

0:42

Gene Music Quartet using Protein Sequence of LRR1 "LEUCINE RICH REPEAT PROTEIN 1"

1:07

Gene Music using Protein Sequence of LRRTM4 "LEUCINE RICH REPEAT TRANSMEMBRANE NEURONAL 4"

0:39

Gene Music Using Protein Sequence of LRR1 "LEUCINE RICH REPEAT PROTEIN 1"

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.
    • Examples 

    • Associated domains