Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/68764
Type: Artigo de periódico
Title: On the quaternary structure of a C-type lectin from Bothrops jararacussu venom - BJ-32 (BjcuL)
Author: Silva, FP
Alexandre, GMC
Ramos, CHI
De-Simone, SG
Abstract: BJ-32 (also known as BjcuL) is a C-type lectin from the venom of Bothrops jararacussu with specificity for beta-galactosides and a remarkable ability to agglutinate several species of trypanosornatids. Our objective was to study the oligomerization state of native BJ-32 by using different biophysical and Computational methods. Small-angle X-ray light scattering (SAXS) experiments disclosed a compact, globular protein with a radius of gyration of 36.72 +/- 0.04 angstrom and molecular weight calculated as 147.5 +/- 2.0 kDa. From analytical ultracentrifugation analysis, it was determined that the BJ-32 sedimentation profile fits nicely to a decamer model. The analysis of the intrinsic emitted fluorescence spectra for BJ-32 solutions indicated that association of subunits in the decamer is accompanied by changes in the environment of Tryptophan residues. Both ab initio and comparative models of BJ-32 supported the resemblance of the decamer in the crystallographic structure from a close homologue, the rattlesnake venom lectin (RSL) from Crotalus atrox. (C) 2008 Published by Elsevier Ltd.
Subject: Oligomerization
Quaternary structure
Solution structure
Snake venom lectin
Country: Inglaterra
Editor: Pergamon-elsevier Science Ltd
Rights: fechado
Identifier DOI: 10.1016/j.toxicon.2008.10.014
Date Issue: 2008
Appears in Collections:Unicamp - Artigos e Outros Documentos

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