3rg1
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==Crystal structure of the RP105/MD-1 complex== | |
| - | + | <StructureSection load='3rg1' size='340' side='right' caption='[[3rg1]], [[Resolution|resolution]] 2.91Å' scene=''> | |
| - | === | + | == Structural highlights == |
| - | {{ | + | <table><tr><td colspan='2'>[[3rg1]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RG1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RG1 FirstGlance]. <br> |
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=PGT:(1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL+STEARATE'>PGT</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CD180 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]), LY86 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rg1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rg1 RCSB], [http://www.ebi.ac.uk/pdbsum/3rg1 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | RP105-MD-1 modulates the TLR4-MD-2-mediated, innate immune response against bacterial lipopolysaccharide (LPS). The crystal structure of the bovine 1:1 RP105-MD-1 complex bound to a putative endogenous lipid at 2.9 A resolution shares a similar overall architecture to its homolog TLR4-MD-2 but assembles into an unusual 2:2 homodimer that differs from any other known TLR-ligand assembly. The homodimer is assembled in a head-to-head orientation that juxtaposes the N-terminal leucine-rich repeats (LRRs) of the two RP105 chains, rather than the usual tail-to-tail configuration of C-terminal LRRs in ligand-activated TLR dimers, such as TLR1-TRL2, TLR2-TLR6, TLR3-TLR3 and TLR4-TLR4. Another unusual interaction is mediated by an RP105-specific asparagine-linked glycan, which wedges MD-1 into the co-receptor binding concavity on RP105. This unique mode of assembly represents a new paradigm for TLR complexes and suggests a molecular mechanism for regulating LPS responses. | ||
| - | + | An unusual dimeric structure and assembly for TLR4 regulator RP105-MD-1.,Yoon SI, Hong M, Wilson IA Nat Struct Mol Biol. 2011 Aug 21;18(9):1028-35. doi: 10.1038/nsmb.2106. PMID:21857663<ref>PMID:21857663</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | < | + | </div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
| - | [[Category: Hong, M | + | [[Category: Hong, M]] |
| - | [[Category: Wilson, I A | + | [[Category: Wilson, I A]] |
| - | [[Category: Yoon, S I | + | [[Category: Yoon, S I]] |
[[Category: Beta-cup-like structure]] | [[Category: Beta-cup-like structure]] | ||
[[Category: Immune regulation]] | [[Category: Immune regulation]] | ||
[[Category: Immune system]] | [[Category: Immune system]] | ||
[[Category: Leucine-rich repeat domain]] | [[Category: Leucine-rich repeat domain]] | ||
Revision as of 08:27, 18 December 2014
Crystal structure of the RP105/MD-1 complex
| |||||||||||
