2evl

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(New page: 200px<br /> <applet load="2evl" size="450" color="white" frame="true" align="right" spinBox="true" caption="2evl, resolution 2.200&Aring;" /> '''Crystal structure ...)
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<applet load="2evl" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2evl, resolution 2.200&Aring;" />
caption="2evl, resolution 2.200&Aring;" />
'''Crystal structure of human Glycolipid Transfer Protein complexed with 18:2 Galactosylceramide'''<br />
'''Crystal structure of human Glycolipid Transfer Protein complexed with 18:2 Galactosylceramide'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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2EVL 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 GAL, SPH, LNK and OCT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2EVL OCA].
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2EVL 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=GAL:'>GAL</scene>, <scene name='pdbligand=SPH:'>SPH</scene>, <scene name='pdbligand=LNK:'>LNK</scene> and <scene name='pdbligand=OCT:'>OCT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EVL OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Abagyan, R.]]
[[Category: Abagyan, R.]]
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[[Category: Brown, R.E.]]
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[[Category: Brown, R E.]]
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[[Category: Kanack, A.T.]]
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[[Category: Kanack, A T.]]
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[[Category: Malakhova, M.L.]]
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[[Category: Malakhova, M L.]]
[[Category: Malinina, L.]]
[[Category: Malinina, L.]]
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[[Category: Patel, D.J.]]
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[[Category: Patel, D J.]]
[[Category: GAL]]
[[Category: GAL]]
[[Category: LNK]]
[[Category: LNK]]
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[[Category: protein-glycolipid complex]]
[[Category: protein-glycolipid complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:56:18 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:14:58 2008''

Revision as of 15:15, 21 February 2008


2evl, resolution 2.200Å

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Crystal structure of human Glycolipid Transfer Protein complexed with 18:2 Galactosylceramide

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

2EVL is a Single protein structure of sequence from Homo sapiens with , , and as ligands. 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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