Structural evidence for adaptive ligand binding of glycolipid transfer protein

A1 Journal article (refereed)


Internal Authors/Editors


Publication Details

List of Authors: Airenne TT, Kidron H, Nymalm Y, Nylund M, West G, Mattjus P, Salminen TA
Publisher: ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD
Publication year: 2006
Journal: Journal of Molecular Biology
Journal acronym: J MOL BIOL
Volume number: 355
Issue number: 2
Start page: 224
End page: 236
Number of pages: 13
ISSN: 0022-2836
eISSN: 1089-8638


Abstract

Glycolipids participate in many important cellular processes and they are bound and transferred with high specificity by glycolipid transfer protein (GLTP). We have solved three different X-ray structures of bovine GLTP at 1.4 angstrom, 1.6 angstrom and 1.8 angstrom resolution, all with a bound fatty acid or glycolipid. The 1.4 A structure resembles the recently characterized apo-form of the human GLTP but the other two structures represent an intermediate conformation of the apo-GLTPs and the human lactosylceramide-bound GLTP structure. These novel structures give insight into the mechanism of lipid binding and how GLTP may conformationally adapt to different lipids. Furthermore, based on the structural comparison of the GLTP structures and the three-dimensional models of the related Podospora anserina HET-C2 and Arabidopsis thaliana accelerated cell death protein, ACD11, we give structural explanations for their specific lipid binding properties.


Keywords

cavity, conformational change, crystal structure, homology modeling

Last updated on 2019-16-07 at 06:42