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 GAL, SPH, LNK and OCT 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 Mon Nov 12 21:56:18 2007
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
