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

Artículos de revistas

Fecha

2007-01-01

Registro en:

Protein and Peptide Letters, v. 14, n. 7, p. 698-701, 2007.

0929-8665

http://hdl.handle.net/11449/130626

10.2174/092986607781483796

WOS:000253577200011

2-s2.0-34548669385

Institución

Universidade Estadual Paulista (Brasil)

Resumen

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.

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