Affordable Access

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

Authors
  • Chevalier, Franck
  • Lopez-Prados, Javier
  • Groves, Patrick
  • Perez, Serge
  • Martín-Lomas, Manuel
  • Nieto, Pedro M
Type
Published Article
Journal
Glycobiology
Publication Date
Oct 01, 2006
Volume
16
Issue
10
Pages
969–980
Identifiers
PMID: 16774909
Source
Medline
License
Unknown

Abstract

A suitable approach which combines nuclear magnetic resonance (NMR) spectroscopy and molecular dynamics (MD) simulations have been used to study the structure and the dynamics of the glycosylphosphatidylinositol (GPI) anchor Manalphal-2Manalpha1-6Manalphal -4GlcNalpha1-6myo-inositol-1-OPO(3)-sn-1,2-dimyristoylglycerol (1) incorporated into dodecylphosphatidylcholine (DPC) 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 nuclear overhauser effect (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.

Report this publication

Statistics

Seen <100 times