On the quaternary structure of a C-type lectin from Bothrops jararacussu venom--BJ-32 (BjcuL).
Toxicon
; 52(8): 944-53, 2008 Dec 15.
Article
em En
| MEDLINE
| ID: mdl-18948130
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 trypanosomatids. 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+/-0.04A and molecular weight calculated as 147.5+/-2.0kDa. 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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Bothrops
/
Venenos de Crotalídeos
/
Lectinas Tipo C
Limite:
Animals
Idioma:
En
Ano de publicação:
2008
Tipo de documento:
Article