The conformation of the C-glycosyl analogue of N-acetyl-lactosamine in the free state and bound to a toxic plant agglutinin and human adhesion/growth-regulatory galectin-1.
Carbohydr Res
; 342(12-13): 1918-28, 2007 Sep 03.
Article
em En
| MEDLINE
| ID: mdl-17408600
ABSTRACT
The conformational behavior of the C-glycoside analogue of N-acetyl-lactosamine, beta-C-Gal-(1-->4)-beta-GlcNAc-OMe, 1, has been studied using a combination of molecular mechanics calculations and NMR spectroscopy (J and NOE data). It is shown that the C-disaccharide populates three distinctive conformational families in solution, the major one being the anti-psi conformation. Of note, this conformation is only marginally populated for the O-disaccharide. Due to its conspicuous role in the regulation of adhesion, growth and tissue invasion of tumors and its avid binding to N-acetyl-lactosamine human, galectin-1 was tested as a receptor. This endogenous lectin recognizes a local minimum of 1, the syn-PhiPsi conformer, and thus a conformational selection process is correlated with the molecular recognition event.
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Base de dados:
MEDLINE
Assunto principal:
Galectina 1
/
Lectinas de Plantas
/
Amino Açúcares
/
Glicosídeos
Limite:
Humans
Idioma:
En
Revista:
Carbohydr Res
Ano de publicação:
2007
Tipo de documento:
Article
País de afiliação:
França