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

Takeda, AAS; dos Santos, J. I.; Marcussi, S.; Silveira, L. B.; Soares, A. M.; Fontes, MRM

Otro

Registro en:

Biochimica Et Biophysica Acta-proteins and Proteomics. Amsterdam: Elsevier B.V., v. 1699, n. 1-2, p. 281-284, 2004.

1570-9639

http://hdl.handle.net/11449/17577

http://acervodigital.unesp.br/handle/11449/17577

10.1016/j.bbapap.2004.02.005

WOS:000221807800030

http://dx.doi.org/10.1016/j.bbapap.2004.02.005

http://repositorioslatinoamericanos.uchile.cl/handle/2250/864027

Autor

Takeda, AAS

dos Santos, J. I.

Marcussi, S.

Silveira, L. B.

Soares, A. M.

Fontes, MRM

Institución

Universidade Paulista Júlio de Mesquita Filho (Brasil)

Resumen

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.

Materias

crystallization

X-ray crystallography

acidic phospholipase A(2)

Bothrops jararacussu venom

alpha-tocopherol

p-bromophenacyl bromide

Mostrar el registro completo del ítem