3v47

Crystal structure of the N-terminal fragment of zebrafish TLR5 in complex with Salmonella flagellin

spinqualitylabelsall models 3v47, resolution 2.47Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3v47 is a 4 chain structure with sequence from Bdellostoma burgeri and Saldu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAG Related: 3v44 Gene: fliC, fliC1 (SALDU) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FLIC_SALDU] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. Publication Abstract from PubMed Toll-like receptor 5 (TLR5) binding to bacterial flagellin activates signaling through the transcription factor NF-kappaB and triggers an innate immune response to the invading pathogen. To elucidate the structural basis and mechanistic implications of TLR5-flagellin recognition, we determined the crystal structure of zebrafish TLR5 (as a variable lymphocyte receptor hybrid protein) in complex with the D1/D2/D3 fragment of Salmonella flagellin, FliC, at 2.47 angstrom resolution. TLR5 interacts primarily with the three helices of the FliC D1 domain using its lateral side. Two TLR5-FliC 1:1 heterodimers assemble into a 2:2 tail-to-tail signaling complex that is stabilized by quaternary contacts of the FliC D1 domain with the convex surface of the opposing TLR5. The proposed signaling mechanism is supported by structure-guided mutagenesis and deletion analyses on CBLB502, a therapeutic protein derived from FliC. Structural basis of TLR5-flagellin recognition and signaling.,Yoon SI, Kurnasov O, Natarajan V, Hong M, Gudkov AV, Osterman AL, Wilson IA Science. 2012 Feb 17;335(6070):859-64. PMID:22344444 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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