3rg1

Crystal structure of the RP105/MD-1 complex

spinqualitylabelsall models 3rg1, resolution 2.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3rg1 is a 16 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.91Å Ligands: BMA, MAN, NAG, PGT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A6QNK7_BOVIN 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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