2EUK
Crystal Structure of Human Glycolipid Transfer Protein complexed with 24:1 Galactosylceramide
Summary for 2EUK
| Entry DOI | 10.2210/pdb2euk/pdb |
| Related | 1SWX 1SX6 |
| Descriptor | Glycolipid transfer protein, beta-D-galactopyranose, SPHINGOSINE, ... (6 entities in total) |
| Functional Keywords | protein-glycolipid complex, lipid transport |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 24838.27 |
| Authors | Malinina, L.,Malakhova, M.L.,Kanack, A.T.,Abagyan, R.,Brown, R.E.,Patel, D.J. (deposition date: 2005-10-28, release date: 2006-11-14, Last modification date: 2023-08-23) |
| Primary citation | Malinina, L.,Malakhova, M.L.,Kanack, A.T.,Lu, M.,Abagyan, R.,Brown, R.E.,Patel, D.J. The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure. Plos Biol., 4:e362-e362, 2006 Cited by PubMed 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. PubMed: 17105344DOI: 10.1371/journal.pbio.0040362 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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