Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/2270
Type: Artigo de periódico
Title: Crystallization and preliminary X-ray diffraction analysis of three myotoxic phospholipases A2 from Bothrops brazili venom
Author: Fernandes, Carlos A. H.
Gartuzo, Elaine C. G.
Pagotto, Ivan
Comparetti, Edson J.
Huancahuire-Vega, Salomon
Ponce-Soto, Luis Alberto
Costa, Tassia R.
Marangoni, Sergio
Soares, Andreimar M.
Fontes, Marcos R. M.
Abstract: Two myotoxic and noncatalytic Lys49-phospholipases A2 (braziliantoxin-II and MT-II) and a myotoxic and catalytic phospholipase A2 (braziliantoxin-III) from the venom of the Amazonian snake Bothrops brazili were crystallized. The crystals diffracted to resolutions in the range 2.562.05 angstrom and belonged to space groups P3121 (braziliantoxin-II), P6522 (braziliantoxin-III) and P21 (MT-II). The structures were solved by molecular-replacement techniques. Both of the Lys49-phospholipases A2 (braziliantoxin-II and MT-II) contained a dimer in the asymmetric unit, while the Asp49-phospholipase A2 braziliantoxin-III contained a monomer in its asymmetric unit. Analysis of the quaternary assemblies of the braziliantoxin-II and MT-II structures using the PISA program indicated that both models have a dimeric conformation in solution. The same analysis of the braziliantoxin-III structure indicated that this protein does not dimerize in solution and probably acts as a monomer in vivo, similar to other snake-venom Asp49-phospholipases A2.
Subject: phospholipases A2
Bothrops brazili
braziliantoxin-II
braziliantoxin-III
MT-II
Editor: Wiley-Blackwell
Citation: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. Wiley-Blackwell, v.68, p.935-938, 2012
Rights: fechado
Identifier DOI: 10.1107/S1744309112026073
Date Issue: 2012
Appears in Collections:IB - Artigos e Outros Documentos

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