2EVD: Crystal structure of human Glycolipid Transfer Protein complexed with 12:0 Lactosylceramide

Citation:
Abstract
Glycosphingolipids (GSLs) play major roles in cellular growth and development. Mammalian glycolipid transfer proteins (GLTPs) are potential regulators of cell processes mediated by GSLs and display a unique architecture among lipid binding/transfer proteins. The GLTP fold represents a novel membrane targeting/interaction domain among peripheral proteins. Here we report crystal structures of human GLTP bound to GSLs of diverse acyl chain length, unsaturation, and sugar composition. Structural comparisons show a highly conserved anchoring of galactosyl- and lactosyl-amide headgroups by the GLTP recognition center. By contrast, acyl chain chemical structure and occupancy of the hydrophobic tunnel dictate partitioning between sphingosine-in and newly-observed sphingosine-out ligand-binding modes. The structural insights, combined with computed interaction propensity distributions, suggest a concerted sequence of events mediated by GLTP conformational changes during GSL transfer to and/or from membranes, as well as during GSL presentation and/or transfer to other proteins.
PDB ID: 2EVDDownload
MMDB ID: 42692
PDB Deposition Date: 2005/10/31
Updated in MMDB: 2006/12
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 2EVD: monomeric; determined by author
Molecular Components in 2EVD
Label Count Molecule
Protein (1 molecule)
1
Glycolipid Transfer Protein(Gene symbol: GLTP)
Molecule annotation
Chemicals (5 molecules)
1
1
2
1
3
1
4
1
5
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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