5HA0
Crystal structure of the LTBP1 leukotriene d4 complex
Summary for 5HA0
| Entry DOI | 10.2210/pdb5ha0/pdb |
| Related | 5H9L 5H9N 5HAE |
| Descriptor | Lipocalin AI-4, (5~{S},6~{R},7~{E},9~{E},11~{Z},14~{Z})-6-[(2~{R})-2-azanyl-3-(2-hydroxy-2-oxoethylamino)-3-oxidanylidene-propyl]sulfanyl-5-oxidanyl-icosa-7,9,11,14-tetraenoic acid (3 entities in total) |
| Functional Keywords | lipocalin, leukotriene, rhodnius, salivary, transport protein |
| Biological source | Rhodnius prolixus (Triatomid bug) |
| Total number of polymer chains | 1 |
| Total formula weight | 17401.37 |
| Authors | Andersen, J.F. (deposition date: 2015-12-29, release date: 2016-05-11, Last modification date: 2023-09-27) |
| Primary citation | Jablonka, W.,Pham, V.,Nardone, G.,Gittis, A.,Silva-Cardoso, L.,Atella, G.C.,Ribeiro, J.M.,Andersen, J.F. Structure and Ligand-Binding Mechanism of a Cysteinyl Leukotriene-Binding Protein from a Blood-Feeding Disease Vector. Acs Chem.Biol., 11:1934-1944, 2016 Cited by PubMed Abstract: 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. PubMed: 27124118DOI: 10.1021/acschembio.6b00032 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.441 Å) |
Structure validation
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