7nux

Crystal structure of the TIR domain of human TLR1 (crystallised without ZN2+ ions)Crystal structure of the TIR domain of human TLR1 (crystallised without ZN2+ ions)

Structural highlights 7nux is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.47Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TLR1_HUMAN Participates in the innate immune response to microbial agents. Specifically recognizes diacylated and triacylated lipopeptides. Cooperates with TLR2 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). Publication Abstract from PubMed Toll-like receptors (TLRs) play an important role in the innate immune response. While a lot is known about the structures of their extracellular parts, many questions are still left unanswered, when the structural basis of TLR activation is analyzed for the TLR intracellular domains. Here we report the structure and dynamics of TLR1 toll-interleukin like (TIR) cytoplasmic domain in crystal and in solution. We found that the TLR1-TIR domain is capable of specific binding of Zn with nanomolar affinity. Interactions with Zn are mediated by cysteine residues 667 and 686 and C667 is essential for the Zn binding. Potential structures of the TLR1-TIR/Zn complex were predicted in silico. Using the functional assays for the heterodimeric TLR1/2 receptor, we found that both Zn addition and Zn depletion affect the activity of TLR1, and C667A mutation disrupts the receptor activity. Analysis of C667 position in the TLR1 structure and possible effects of C667A mutation, suggests that zinc-binding ability of TLR1-TIR domain is critical for the receptor activation. Modulation of Toll-like receptor 1 intracellular domain structure and activity by Zn(2+) ions.,Lushpa VA, Goncharuk MV, Lin C, Zalevsky AO, Talyzina IA, Luginina AP, Vakhrameev DD, Shevtsov MB, Goncharuk SA, Arseniev AS, Borshchevskiy VI, Wang X, Mineev KS Commun Biol. 2021 Aug 24;4(1):1003. doi: 10.1038/s42003-021-02532-0. PMID:34429510 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Toll-like Receptor 3D structures

spinqualitylabelsall models 7nux, resolution 2.47Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image