5h9l

Crystal Structure of LTBP1 in complex with cleaved Leukotriene C4

spinqualitylabelsall models 5h9l, resolution 1.37Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5h9l is a 1 chain structure with sequence from Rhodnius prolixus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.37Å Ligands: EAH, GSH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q7YT09_RHOPR Publication Abstract from PubMed Blood-feeding disease vectors mitigate the negative effects of hemostasis and inflammation through the binding of small-molecule agonists of these processes by salivary proteins. In this study, a lipocalin protein family member (LTBP1) from the saliva of Rhodnius prolixus, a vector of the pathogen Trypanosoma cruzi, is shown to sequester cysteinyl leukotrienes during feeding to inhibit immediate inflammatory responses. Calorimetric binding experiments showed that LTBP1 binds leukotrienes C4 (LTC4), D4 (LTD4), and E4 (LTE4) but not biogenic amines, adenosine diphosphate, or other eicosanoid compounds. Crystal structures of ligand-free LTBP1 and its complexes with LTC4 and LTD4 reveal a conformational change during binding that brings Tyr114 into close contact with the ligand. LTC4 is cleaved in the complex, leaving free glutathione and a C20 fatty acid. Chromatographic analysis of bound ligands showed only intact LTC4, suggesting that cleavage could be radiation-mediated. Structure and Ligand-Binding Mechanism of a Cysteinyl Leukotriene-Binding Protein from a Blood-Feeding Disease Vector.,Jablonka W, Pham V, Nardone G, Gittis A, Silva-Cardoso L, Atella GC, Ribeiro JM, Andersen JF ACS Chem Biol. 2016 May 12. PMID:27124118 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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