3V44

Crystal structure of the N-terminal fragment of zebrafish TLR5

Summary for 3V44

• Entry DOI: 10.2210/pdb3v44/pdb
• Related: 3V47
• Descriptor: Toll-like receptor 5b and variable lymphocyte receptor B.61 chimeric protein, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: flagellin, innate immunity, leucine-rich repeat, innate immune receptor, immune system
• Biological source: Danio rerio (zebra fish, inshore hagfish); More
• Total number of polymer chains: 1
• Total formula weight: 46382.67

Authors

Yoon, S.I.,Hong, H.,Wilson, I.A. (deposition date: 2011-12-14, release date: 2012-02-29, Last modification date: 2024-10-16)

Primary citation

Yoon, S.I.,Kurnasov, O.,Natarajan, V.,Hong, M.,Gudkov, A.V.,Osterman, A.L.,Wilson, I.A.
Structural basis of TLR5-flagellin recognition and signaling.
Science, 335:859-864, 2012

PubMed Abstract: Toll-like receptor 5 (TLR5) binding to bacterial flagellin activates signaling through the transcription factor NF-κB 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.

PubMed: 22344444
DOI: 10.1126/science.1215584

Experimental method

X-RAY DIFFRACTION (2.83 Å)