Structural analysis of ConBr reveals molecular correlation between the carbohydrate recognition domain and endothelial NO synthase activation.

Abstract:

:Diocleinae lectins are highly homologous in their primary structure which features metal binding sites and a carbohydrate recognition domain (CRD). Differences in the biological activity of legume lectins have been widely investigated using hemagglutination inhibition assays, isothermal titration microcalorimetry and co-crystallization with mono- and oligosaccharides. Here we report a new lectin crystal structure (ConBr) extracted from seeds of Canavalia brasiliensis, predict dimannoside binding by docking, identify the α-aminobutyric acid (Abu) binding pocket and compare the CRD of ConBr to that of homologous lectins. Based on the hypothesis that the carbohydrate affinity of lectins depends on CRD configuration, the relationship between tridimensional structure and endothelial NO synthase activation was used to clarify differences in biological activity. Our study established a correlation between the position of CRD amino acid side chains and the stimulation of NO release from endothelium.

authors

Bezerra EH,Rocha BA,Nagano CS,Bezerra Gde A,Moura TR,Bezerra MJ,Benevides RG,Sampaio AH,Assreuy AM,Delatorre P,Cavada BS

doi

10.1016/j.bbrc.2011.04.061

subject

Has Abstract

pub_date

2011-05-20 00:00:00

pages

566-70

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(11)00646-2

journal_volume

408

pub_type

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