2evl
From Proteopedia
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Crystal structure of human Glycolipid Transfer Protein complexed with 18:2 Galactosylceramide
Overview
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.
About this Structure
2EVL is a Single protein structure of sequence from Homo sapiens with , , and as ligands. Full crystallographic information is available from OCA.
Reference
The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure., Malinina L, Malakhova ML, Kanack AT, Lu M, Abagyan R, Brown RE, Patel DJ, PLoS Biol. 2006 Nov;4(11):e362. PMID:17105344
Page seeded by OCA on Thu Feb 21 17:14:58 2008
Categories: Homo sapiens | Single protein | Abagyan, R. | Brown, R E. | Kanack, A T. | Malakhova, M L. | Malinina, L. | Patel, D J. | GAL | LNK | OCT | SPH | Protein-glycolipid complex
