Leucine-rich repeat

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The leucine-rich repeat (LRR) proteins are a large family of over 60,000 proteins found in viruses, bacteria, archaea, and eukaryotes that feature horseshoe- or arc-shaped domains made of leucine-rich repeating motifs.[1] Presently, at least 144 structures with leucine-rich repeats are deposited at the RCSB Protein Data Bank.[2]

 

Lamprey Variable Lymphocyte Receptor bound to a trisaccharide antigen (3e6j), resolution 1.67Å



 

Articles in Proteopedia concerning Leucine-rich repeat proteins include:


To view automatically seeded indices concerning Leucine-rich repeat proteins[3][4], see:


Contents

References and Notes

  1. Matsushima N, Miyashita H, Mikami T, Kuroki Y. A nested leucine rich repeat (LRR) domain: the precursor of LRRs is a ten or eleven residue motif. BMC Microbiol. 2010 Sep 9;10:235. PMID:20825685 doi:10.1186/1471-2180-10-235
  2. LRRML Database (Version 1.6: Released November 25, 2010): Conformational LRR XML-Database at http://tollml.lrz.de:8081/exist/rest//lrrml/releases/releases.xq
  3. Matsushima N, Miyashita H, Mikami T, Kuroki Y. A nested leucine rich repeat (LRR) domain: the precursor of LRRs is a ten or eleven residue motif. BMC Microbiol. 2010 Sep 9;10:235. PMID:20825685 doi:10.1186/1471-2180-10-235
  4. LRRML Database (Version 1.6: Released November 25, 2010): Conformational LRR XML-Database at http://tollml.lrz.de:8081/exist/rest//lrrml/releases/releases.xq

See Also

Additional Literature

  • Kobe B, Kajava AV. The leucine-rich repeat as a protein recognition motif. Curr Opin Struct Biol. 2001 Dec;11(6):725-32. PMID:11751054
  • Matsushima N, Tanaka T, Enkhbayar P, Mikami T, Taga M, Yamada K, Kuroki Y. Comparative sequence analysis of leucine-rich repeats (LRRs) within vertebrate toll-like receptors. BMC Genomics. 2007 May 21;8:124. PMID:17517123 doi:10.1186/1471-2164-8-124
  • Istomin AY, Godzik A. Understanding diversity of human innate immunity receptors: analysis of surface features of leucine-rich repeat domains in NLRs and TLRs. BMC Immunol. 2009 Sep 3;10:48. PMID:19728889 doi:10.1186/1471-2172-10-48
  • Matsushima N, Tachi N, Kuroki Y, Enkhbayar P, Osaki M, Kamiya M, Kretsinger RH. Structural analysis of leucine-rich-repeat variants in proteins associated with human diseases. Cell Mol Life Sci. 2005 Dec;62(23):2771-91. PMID:16231091 doi:10.1007/s00018-005-5187-z
  • Kajava AV, Kobe B. Assessment of the ability to model proteins with leucine-rich repeats in light of the latest structural information. Protein Sci. 2002 May;11(5):1082-90. PMID:11967365 doi:10.1110/ps.4010102
  • Jin MS, Lee JO. Application of hybrid LRR technique to protein crystallization. BMB Rep. 2008 May 31;41(5):353-7. PMID:18510864
  • Carpenter S, O'Neill LA. Recent insights into the structure of Toll-like receptors and post-translational modifications of their associated signalling proteins. Biochem J. 2009 Jul 29;422(1):1-10. PMID:19627256 doi:10.1042/BJ20090616
  • Wei T, Gong J, Jamitzky F, Heckl WM, Stark RW, Rossle SC. LRRML: a conformational database and an XML description of leucine-rich repeats (LRRs). BMC Struct Biol. 2008 Nov 5;8:47. PMID:18986514 doi:10.1186/1472-6807-8-47
  • Gong J, Wei T, Zhang N, Jamitzky F, Heckl WM, Rossle SC, Stark RW. TollML: a database of toll-like receptor structural motifs. J Mol Model. 2010 Jul;16(7):1283-9. Epub 2010 Jan 19. PMID:20084417 doi:10.1007/s00894-009-0640-9

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