Preliminary X-ray crystallographic studies of a Lys49-phospholipase A(2) homologue from Bothrops pirajai venom complexed with p-bromophenacyl bromide and alpha-tocopherol inhibitors

PrTX-I, a non-catalytic and myotoxic Lys49-PLA(2) from Bothrops pirajai venom has been crystallized alone and in complex with bromophenacyl bromide (BPB), alpha-tocopherol and alpha-tocopherol acetate inhibitors. These crystals have shown to diffract X-rays between 2.34 and 1.65 angstrom resolution. All complexes crystals are isomorphous and belong to the space group P2(1) whereas native PrTX-I crystals belong to the P3(1)21.

Palavras-chave

α-tocopherol, Bothrops pirajai venom, Crystallization, Lys49-phospholipase A2, Myotoxity, p-BPB, P-bromophenacyl bromide, Vitamin E, X-ray crystallography, Alpha tocopherol, Bromide, Enzyme inhibitor, Lysine, Phospholipase A, Snake venom, Animal, Chemical structure, Chemistry, Protein conformation, Snake, X ray crystallography, Alpha-Tocopherol, Animals, Bothrops, Bromides, Crotalid Venoms, Crystallography, X-Ray, Enzyme Inhibitors, Lysine, Models, Molecular, Phospholipases A, Protein Conformation, Bothrops pirajai