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|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.
Comparetti, Edson J.
Ponce-Soto, Luis Alberto
Costa, Tassia R.
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.|
|Citation:||Acta Crystallographica Section F: Structural Biology and Crystallization Communications. Wiley-Blackwell, v.68, p.935-938, 2012|
|Appears in Collections:||IB - Artigos e Outros Documentos|
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