Glycolipid transfer proteins

A1 Originalartikel i en vetenskaplig tidskrift (referentgranskad)

Interna författare/redaktörer

Publikationens författare: Brown RE, Mattjus P
Publiceringsår: 2007
Tidskrift: Biochimica et Biophysica Acta Molecular and Cell Biology of Lipids
Tidskriftsakronym: BBA-MOL CELL BIOL L
Volym: 1771
Nummer: 6
Artikelns första sida, sidnummer: 746
Artikelns sista sida, sidnummer: 760
Antal sidor: 15
ISSN: 1388-1981


Glycolipid transfer proteins (GLTPs) are small (24 kDa), soluble, ubiquitous proteins characterized by their ability to accelerate the intermembrane transfer of glycolipids in vitro. GLTP specificity encompasses both sphingoid- and glycerol-based glycolipids, but with a strict requirement that the initial sugar residue be beta-linked to the hydrophobic lipid backbone. The 3D architecture of GLTP reveals liganded structures with unique lipid-binding modes. The biochemical properties of GLTP action at the membrane surface have been studied rather comprehensively, but the biological role of GLTP remains enigmatic. What is clear is that GLTP differs distinctly from other known glycolipid-binding proteins, such as nonspecific lipid transfer proteins, lysosomal sphingolipid activator proteins, lectins, lung surfactant proteins as well as other lipid-binding/transfer proteins. Based on the unique conformational architecture that targets GLTP to membranes and enables glycolipid binding, GLTP is now considered the prototypical and founding member of a new protein superfamily in eukaryotes.


ACD11, cerebroside, cholesterol, FAPP2, ganglioside, GLTP, glycosphingolipid, HET-C2, lipid transfer protein structure, membrane interaction inotif, phosphatidyleholine, sphingomyelin

Senast uppdaterad 2019-11-12 vid 03:48