2evt
From Proteopedia
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| - | [[Image:2evt.gif|left|200px]] | + | [[Image:2evt.gif|left|200px]] |
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| - | '''Crystal structure of D48V mutant of human Glycolipid Transfer Protein''' | + | {{Structure |
| + | |PDB= 2evt |SIZE=350|CAPTION= <scene name='initialview01'>2evt</scene>, resolution 1.990Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=HEX:HEXANE'>HEX</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Crystal structure of D48V mutant of human Glycolipid Transfer Protein''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2EVT is a [ | + | 2EVT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EVT OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for glycosphingolipid transfer specificity., Malinina L, Malakhova ML, Teplov A, Brown RE, Patel DJ, Nature. 2004 Aug 26;430(7003):1048-53. PMID:[http:// | + | Structural basis for glycosphingolipid transfer specificity., Malinina L, Malakhova ML, Teplov A, Brown RE, Patel DJ, Nature. 2004 Aug 26;430(7003):1048-53. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15329726 15329726] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: d48v mutant human gltp]] | [[Category: d48v mutant human gltp]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:44:58 2008'' |
Revision as of 14:44, 20 March 2008
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| , resolution 1.990Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of D48V mutant of human Glycolipid Transfer Protein
Overview
Lipid transfer proteins are important in membrane vesicle biogenesis and trafficking, signal transduction and immunological presentation processes. The conserved and ubiquitous mammalian glycolipid transfer proteins (GLTPs) serve as potential regulators of cell processes mediated by glycosphingolipids, ranging from differentiation and proliferation to invasive adhesion, neurodegeneration and apoptosis. Here we report crystal structures of apo-GLTP (1.65 A resolution) and lactosylceramide-bound (1.95 A) GLTP, in which the bound glycosphingolipid is sandwiched, after adaptive recognition, within a previously unknown two-layer all-alpha-helical topology. Glycosphingolipid binding specificity is achieved through recognition and anchoring of the sugar-amide headgroup to the GLTP recognition centre by hydrogen bond networks and hydrophobic contacts, and encapsulation of both lipid chains, in a precisely oriented manner within a 'moulded-to-fit' hydrophobic tunnel. A cleft-like conformational gating mechanism, involving two interhelical loops and one alpha-helix of GLTP, could enable the glycolipid chains to enter and leave the tunnel in the membrane-associated state. Mutation and functional analyses of residues in the glycolipid recognition centre and within the hydrophobic tunnel support a framework for understanding how GLTPs acquire and release glycosphingolipids during lipid intermembrane transfer and presentation processes.
About this Structure
2EVT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for glycosphingolipid transfer specificity., Malinina L, Malakhova ML, Teplov A, Brown RE, Patel DJ, Nature. 2004 Aug 26;430(7003):1048-53. PMID:15329726
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