Structural principles of leucine‐rich repeat (LRR) proteins
作者： Purevjav Enkhbayar , Masakatsu Kamiya , Mitsuru Osaki , Takeshi Matsumoto , Norio Matsushima
DOI: 10.1002/PROT.10605
关键词:
摘要: LRR-containing proteins are present in over 2000 from viruses to eukaryotes. Most LRRs 20-30 amino acids long, and the repeat number ranges 2 42. The known structures of 14 LRR proteins, each containing 4-17 repeats, have revealed that domains fold into a horseshoe (or arc) shape with parallel beta-sheet on concave face various secondary structures, including alpha-helix, 3(10)-helix, pII helix convex face. We developed simple methods charactere quantitatively arc then applied them all proteins. A quantity 2Rsin(phi/2), which R phi radii rotation angle about central axis per repeating unit, respectively, is highly conserved regardless large variety radius arc. beta-alpha structural units smaller than those beta-3(10) or beta-pII units. forms surface analogous part Mobius strip.
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