title: Structural principles of leucine-rich repeat (LRR) proteins.
abstract: LRR-containing proteins are present in over 2000 proteins from viruses to eukaryotes. Most LRRs are 20-30 amino acids long, and the repeat number ranges from 2 to 42. The known structures of 14 LRR proteins, each containing 4-17 repeats, have revealed that the LRR domains fold into a horseshoe (or arc) shape with a parallel beta-sheet on the concave face and with various secondary structures, including alpha-helix, 3(10)-helix, and pII helix on the convex face. We developed simple methods to charactere quantitatively the arc shape of LRR and then applied them to all known LRR proteins. A quantity of 2Rsin(phi/2), in which R and phi are the radii of the LRR arc and the rotation angle about the central axis per repeating unit, respectively, is highly conserved in all the LRR proteins regardless of a large variety of repeat number and the radius of the LRR arc. The radii of the LRR arc with beta-alpha structural units are smaller than those with beta-3(10) or beta-pII units. The concave face of the LRR beta-sheet forms a surface analogous to a part of a Möbius strip.
authors.affiliation: Division of Biological Resources and Production, Graduate School of Agriculture, Hokkaido University, Sapporo, Hokkaido, Japan.
authors.forename: Purevjav
authors.initials: P
authors.lastname: Enkhbayar
authors.forename: Masakatsu
authors.initials: M
authors.lastname: Kamiya
authors.forename: Mitsuru
authors.initials: M
authors.lastname: Osaki
authors.forename: Takeshi
authors.initials: T
authors.lastname: Matsumoto
authors.forename: Norio
authors.initials: N
authors.lastname: Matsushima
mesh_terms: D020816:Amino Acid Motifs; D000818:Animals; D016384:Consensus Sequence; D006801:Humans; D007930:Leucine / Q000737:chemistry*; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D020449:Repetitive Sequences, Amino Acid
chemical_list: D011506:Proteins; D007930:Leucine