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| [[Image:2evd.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2evd| PDB=2evd | SCENE= }} | | {{STRUCTURE_2evd| PDB=2evd | SCENE= }} |
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| '''Crystal structure of human Glycolipid Transfer Protein complexed with 12:0 Lactosylceramide'''
| | ===Crystal structure of human Glycolipid Transfer Protein complexed with 12:0 Lactosylceramide=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17105344}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17105344 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17105344}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Patel, D J]] | | [[Category: Patel, D J]] |
| [[Category: Protein-glycolipid complex]] | | [[Category: Protein-glycolipid complex]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:09:23 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:49:40 2008'' |
