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Hydrogen bonding geometry of a protein-bound carbohydrate from water exchange-mediated cross-relaxation.

Authors :
Sayers EW
Weaver JL
Prestegard JH
Source :
Journal of biomolecular NMR [J Biomol NMR] 1998 Aug; Vol. 12 (2), pp. 209-22.
Publication Year :
1998

Abstract

We present heteronuclear two-dimensional methods for the analysis of the geometry of exchangeable protons on a protein-bound carbohydrate. By using a water-selective NOESY-HSQC, we observed cross-relaxation between carbohydrate hydroxyl protons and non-exchangeable ring protons in the complex of [13C6]-alpha-methyl-D-mannopyranoside with recombinant rat mannose binding protein. Using a simple kinetic model, we were able to explain the differences in the initial slopes of the resulting cross-relaxation buildup curves in terms of the geometry of the hydroxyl protons in the bound state. The hydroxyl rotamers consistent with our cross-relaxation data fit very well with predictions based on the crystal structure of MBP bound to a mannose-rich oligosaccharide. These methods should be applicable to other systems where both ligand exchange and water exchange are fast relative to the rate of cross-relaxation.

Details

Language :
English
ISSN :
0925-2738
Volume :
12
Issue :
2
Database :
MEDLINE
Journal :
Journal of biomolecular NMR
Publication Type :
Academic Journal
Accession number :
9751995
Full Text :
https://doi.org/10.1023/a:1008220522409