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Structural basis for glycosphingolipid transfer specificity.

Lucy Malinina¹, Margarita L Malakhova, Alexei Teplov

¹Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.

|August 27, 2004

Summary

Mammalian glycolipid transfer proteins (GLTPs) bind glycosphingolipids using a unique helical structure. This mechanism explains how GLTPs transfer lipids between membranes, impacting cell processes.

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Area of Science:

Structural biology
Biochemistry
Cell biology

Background:

Lipid transfer proteins (LTPs) are crucial for membrane dynamics, including vesicle trafficking and signal transduction.
Mammalian glycolipid transfer proteins (GLTPs) regulate cell functions via glycosphingolipids, affecting processes like differentiation, proliferation, and neurodegeneration.

Purpose of the Study:

To elucidate the structural basis of glycosphingolipid binding and transfer by mammalian GLTPs.
To understand the molecular mechanisms underlying GLTP's role in lipid-mediated cellular processes.

Main Methods:

X-ray crystallography was used to determine the structures of apo-GLTP and lactosylceramide-bound GLTP at high resolution (1.65 Å and 1.95 Å, respectively).
Mutational and functional analyses were performed on key residues within the GLTP structure.

Main Results:

The crystal structures reveal a novel two-layer all-alpha-helical topology where glycosphingolipids are bound.
Glycosphingolipid specificity is determined by hydrogen bonding and hydrophobic interactions at the GLTP recognition center and lipid chain encapsulation within a hydrophobic tunnel.
A cleft-like conformational gating mechanism involving interhelical loops and an alpha-helix facilitates lipid entry and exit.

Conclusions:

The study provides a structural framework for understanding how GLTPs bind and release glycosphingolipids.
This mechanism is essential for lipid intermembrane transfer and presentation, offering insights into GLTP's regulatory roles in cellular processes.