Structural evidence for adaptive ligand binding of glycolipid transfer protein

A1 Originalartikel i en vetenskaplig tidskrift (referentgranskad)


Interna författare/redaktörer


Publikationens författare: Airenne TT, Kidron H, Nymalm Y, Nylund M, West G, Mattjus P, Salminen TA
Förläggare: ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD
Publiceringsår: 2006
Tidskrift: Journal of Molecular Biology
Tidskriftsakronym: J MOL BIOL
Volym: 355
Nummer: 2
Artikelns första sida, sidnummer: 224
Artikelns sista sida, sidnummer: 236
Antal sidor: 13
ISSN: 0022-2836
eISSN: 1089-8638


Abstrakt

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.


Nyckelord

cavity, conformational change, crystal structure, homology modeling

Senast uppdaterad 2019-15-10 vid 02:46