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| - | [[Image:2evt.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2evt| PDB=2evt | SCENE= }} | | {{STRUCTURE_2evt| PDB=2evt | SCENE= }} |
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| - | '''Crystal structure of D48V mutant of human Glycolipid Transfer Protein'''
| + | ===Crystal structure of D48V mutant of human Glycolipid Transfer Protein=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15329726}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15329726 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15329726}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Teplov, A.]] | | [[Category: Teplov, A.]] |
| | [[Category: D48v mutant human gltp]] | | [[Category: D48v mutant human gltp]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:10:15 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:00:17 2008'' |
Revision as of 09:00, 28 July 2008
Template:STRUCTURE 2evt
Crystal structure of D48V mutant of human Glycolipid Transfer Protein
Template:ABSTRACT PUBMED 15329726
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
Page seeded by OCA on Mon Jul 28 12:00:17 2008
