6mqf | pdb_00006mqf

Myotoxin II from Bothrops moojeni complexed with Acetylsalicylic acid

spinqualitylabelsall models 6mqf, resolution 1.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6mqf is a 2 chain structure with sequence from Bothrops moojeni. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.693Å Ligands: AIN, DMS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PA2H2_BOTMO Snake venom phospholipase A2 homolog that lack enzymatic activity. Displays myotoxin and edema-inducing activities. Publication Abstract from PubMed Ophidian accidents are considered an important neglected tropical disease by the World Health Organization. Particularly in Latin America, Bothrops snakes are responsible for the majority of the snakebite envenomings that are not efficiently treated by conventional serum therapy. Thus, the search for simple and efficient inhibitors to complement this therapy is a promising research area, and a combination of functional and structural assays have been used to test candidate ligands against specific ophidian venom compounds. Herein, we tested a commercial drug (acetylsalicylic acid, ASA) and a plant compound with antiophidian properties (rosmarinic acid, RA) using myographic, crystallographic and bioinformatics experiments with a phospholipase A2-like toxin, MjTX-II. MjTX-II/RA and MjTX-II/ASA crystal structures were solved at high resolution and revealed the presence of ligands bound to different regions of the toxin. However, in vitro myographic assays showed that only RA is able to prevent the myotoxic effects of MjTX-II. In agreement with functional results, molecular dynamics simulations showed that the RA molecule remains tightly bound to the toxin throughout the calculations, whereas ASA molecules tend to dissociate. This approach aids the design of effective inhibitors of PLA2-like toxins and, eventually, may complement serum therapy. Search for efficient inhibitors of myotoxic activity induced by ophidian phospholipase A2-like proteins using functional, structural and bioinformatics approaches.,Salvador GHM, Cardoso FF, Gomes AA, Cavalcante WLG, Gallacci M, Fontes MRM Sci Rep. 2019 Jan 24;9(1):510. doi: 10.1038/s41598-018-36839-6. PMID:30679550 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phospholipase A2 homolog

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