These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Conformational behavior of alpha-D-mannopyranosyl-(1-->6)-alpha,beta-D-mannose complexed with two mannose-binding plant lectins, Allium sativam agglutinin I and concanavalin A, using NMR and molecular modeling techniques.
    Author: Mazumder P, Mukhopadhyay C.
    Journal: Carbohydr Res; 2010 Jan 11; 345(1):61-7. PubMed ID: 19892324.
    Abstract:
    Herein, we report the intrinsic conformational preferences of alpha-d-Manp-(1-->6)-alpha,beta-d-Manp, (1) in the free state and as two (ASAI and ConA) lectin-bound forms. NMR spectroscopy and molecular dynamics techniques are used as 3D-structural determination tools. In free form disaccharide 1 displays a fair amount of conformational freedom, with one major (phi/psi 95 +/- 30 degrees/195 +/- 20 degrees and one minor (95 +/- 30 degrees/70 +/- 20 degrees) conformations around the glycosidic linkage and around the omega angle, both the gg and gt rotamers are almost equally populated. This is a first report of a three-dimensional structure of 1 bound with ASAI. Both lectins recognize a major phi/psi 95 +/- 30 degrees/200 +/- 30 degrees conformer with the ligand showing more flexibility in the binding site of ConA. Comparison of the mode of binding of the two lectins explains the differences in observed specificities.
    [Abstract] [Full Text] [Related] [New Search]