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Leucine-rich repeat

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A large family of over 60,000 proteins found in viruses, bacteria, archaea, and eukaryotes that feature horseshoe- or arc-shaped domains made of a repeating motif called the leucine-rich repeats because the repeated motif always contains leucine.<ref>PMID: 20825685</ref>
A large family of over 60,000 proteins found in viruses, bacteria, archaea, and eukaryotes that feature horseshoe- or arc-shaped domains made of a repeating motif called the leucine-rich repeats because the repeated motif always contains leucine.<ref>PMID: 20825685</ref>
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[[Image:1m10.jpg|330px|left|thumb| The human leucine-rich repeat family member Glycoprotein Ib alpha involved in Willebrand disease bound to the von Willebrand Factor A1 Domain [[1m10]]]]
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{{Template:Lrrapplet1}}
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{{Structure
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|PDB= 3e6j |SIZE=350|SCENE=Lamprey_Variable_Lymphocyte_Receptor/Ncrainbow/1|CAPTION= Lamprey Variable Lymphocyte Receptor bound to a trisaccharide antigen ([[3e6j]]), resolution 1.67&Aring; <br>(<scene name='Lamprey_Variable_Lymphocyte_Receptor/Leucines_highlighted/1'>highlight leucines</scene>)(<scene name='Lamprey_Variable_Lymphocyte_Receptor/Ncrainbow/1'>initial scene</scene>)
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3e6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e6j OCA], [http://www.ebi.ac.uk/pdbsum/3e6j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3e6j RCSB]</span>
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Revision as of 13:45, 24 November 2010

A large family of over 60,000 proteins found in viruses, bacteria, archaea, and eukaryotes that feature horseshoe- or arc-shaped domains made of a repeating motif called the leucine-rich repeats because the repeated motif always contains leucine.[1]


 

Drag the structure with the mouse to rotate
Lamprey Variable Lymphocyte Receptor bound to a trisaccharide antigen (3e6j), resolution 1.67Å



to get a sense of the repeats.


 

Articles in Proteopedia concerning Leucine-rich repeat proteins include:



PDB ID 1xwd

Drag the structure with the mouse to rotate
Dimer of Hormone Binding Domain of Human Follicle Stimulating Hormone Receptor Bound to Hormone (1xwd), resolution 2.92Å
Ligands: , ,
Gene: CGA (Homo sapiens), FSHB (Homo sapiens), FSHR (Homo sapiens)
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


To view automatically seeded indices concerning Leucine-rich repeat proteins, see:

References

  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

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
  • 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

Proteopedia Page Contributors and Editors (what is this?)

Wayne Decatur, Jaime Prilusky, Michal Harel

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