2evs

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[[Image:2evs.gif|left|200px]]<br /><applet load="2evs" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2evs.gif|left|200px]]
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caption="2evs, resolution 2.200&Aring;" />
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'''Crystal structure of human Glycolipid Transfer Protein complexed with n-hexyl-beta-D-glucoside'''<br />
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{{Structure
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|PDB= 2evs |SIZE=350|CAPTION= <scene name='initialview01'>2evs</scene>, resolution 2.200&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=HEX:HEXANE'>HEX</scene> and <scene name='pdbligand=D10:DECANE'>D10</scene>
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|ACTIVITY=
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|GENE= GLTP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal structure of human Glycolipid Transfer Protein complexed with n-hexyl-beta-D-glucoside'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2EVS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=GLC:'>GLC</scene>, <scene name='pdbligand=HEX:'>HEX</scene> and <scene name='pdbligand=D10:'>D10</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EVS OCA].
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2EVS 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=2EVS OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17105344 17105344]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17105344 17105344]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: protein complex with detergent]]
[[Category: protein complex with detergent]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:15:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:45:00 2008''

Revision as of 14:45, 20 March 2008


PDB ID 2evs

Drag the structure with the mouse to rotate
, resolution 2.200Å
Ligands: , and
Gene: GLTP (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



Crystal structure of human Glycolipid Transfer Protein complexed with n-hexyl-beta-D-glucoside


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

2EVS is a Single protein structure of sequence from Homo sapiens. 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

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