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


Autoria(s): Takeda, AAS; dos Santos, J. I.; Marcussi, S.; Silveira, L. B.; Soares, A. M.; Fontes, MRM
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

20/05/2014

20/05/2014

01/06/2004

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.

Formato

281-284

Identificador

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

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

10.1016/j.bbapap.2004.02.005

WOS:000221807800030

Idioma(s)

eng

Publicador

Elsevier B.V.

Relação

Biochimica et Biophysica Acta: Proteins and Proteomics

Direitos

closedAccess

Palavras-Chave #crystallization #X-ray crystallography #acidic phospholipase A(2) #Bothrops jararacussu venom #alpha-tocopherol #p-bromophenacyl bromide
Tipo

info:eu-repo/semantics/article