Crystallization and preliminary X-ray diffraction analysis of an acidic phospholipase A(2) complexed with p-bromophenacyl bromide and alpha-tocopherol inhibitors at 1.9-and 1.45-A resolution
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Data
2004-06-01
Autores
Takeda, AAS
dos Santos, J. I.
Marcussi, S.
Silveira, L. B.
Soares, A. M.
Fontes, MRM
Título da Revista
ISSN da Revista
Título de Volume
Editor
Elsevier B.V.
Resumo
An acidic phospholipase A(2) (PLA(2)) isolated from Bothrops jararacussu snake venom was crystallized with two inhibitors: alpha-tocopherol (vitamin E) and p-bromophenacyl bromide (BPB). The crystals diffracted at 1.45- and 1.85-Angstrom resolution, respectively, for the complexes with alpha-tocopherol and p-bromophenacyl bromide. The crystals are not isomorphous with those of the native protein, suggesting the inhibitors binding was successful and changes in the quaternary structure may have occurred. (C) 2004 Elsevier B.V. All rights reserved.
Descrição
Palavras-chave
crystallization, X-ray crystallography, acidic phospholipase A(2), Bothrops jararacussu venom, alpha-tocopherol, p-bromophenacyl bromide
Como citar
Biochimica Et Biophysica Acta-proteins and Proteomics. Amsterdam: Elsevier B.V., v. 1699, n. 1-2, p. 281-284, 2004.