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
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Data
2007-01-01
Autores
Santos, Juliana I. dos [UNESP]
Marchi-Salvador, Daniela P. [UNESP]
Fernandes, Carlos A. H. [UNESP]
Silveira, Lucas B.
Soares, Andreimar M.
Fontes, Marcos R. M. [UNESP]
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Título de Volume
Editor
Bentham Science Publ Ltd
Resumo
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.
Descrição
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
Como citar
Protein and Peptide Letters, v. 14, n. 7, p. 698-701, 2007.