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Glycobiology Advance Access published online on June 14, 2006
Glycobiology, doi:10.1093/glycob/cwl015
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© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Article

Structure and dynamics of the conserved protein GPI anchor core inserted into detergent micelles

Franck Chevalier 1, Javier Lopez-Prados 2, Patrick Groves 3, Serge Perez 4, Manuel Martín-Lomas 2, and Pedro M. Nieto 2 *

1 Grupo de Carbohidratos, Instituto de Investigaciones Químicas, CSIC, Isla de la Cartuja, C/Américo Vespucio 49, 41092 Seville, Spain; Centre de Recherches sur les Macromolécules Végétales (CERMAV), CNRS, BP 53F-38941 Grenoble cedex 9, France
2 Grupo de Carbohidratos, Instituto de Investigaciones Químicas, CSIC, Isla de la Cartuja, C/Américo Vespucio 49, 41092 Seville, Spain
3 Centro de Investigaciones Biologicas, CSIC C/Ramiro de Maeztu 9, 28040 Madrid, Spain
4 Centre de Recherches sur les Macromolécules Végétales (CERMAV), CNRS, BP 53F-38941 Grenoble cedex 9, France

* To whom correspondence should be addressed.
Pedro M. Nieto, E-mail: pedro.nieto{at}iiq.csic.es


  Abstract

A suitable approach which combines NMR spectroscopy and molecular dynamics (MD) simulations have been used to study the structure and the dynamics of the glycosylphosphatidylinositol (GPI) anchor 1 incorporated into dodecylphosphatidylcholine micelles. The results have been compared to those previously obtained for the products obtainable from 1 after phospholipase cleavage, in aqueous solution. Relaxation and diffusion NMR experiments were used to establish the formation of stable aggregates and the insertion of 1 into the micelles. MD calculations were performed including explicit water, sodium and chloride ions and using the Particle Mesh Ewald approach for the evaluation of the electrostatic energy term. The MD predicted three dimensional structure and dynamics were substantiated by NOE measurements and relaxation data. The pseudopentasaccharide structure, which was not affected by incorporation of 1 into the micelle, showed a complex dynamic behaviour with a faster relative motion at the terminal mannopyranose unit and decreased mobility close to the micelle. This motion may be better described as an oscillation relative to the membrane rather than a folding event.

Keywords: GPI anchor / Conformational analysis/ Molecular Flexibility/ Molecular modelling / NMR spectroscopy/ micelle.
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