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1zt4

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(New page: 200px<br /> <applet load="1zt4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zt4, resolution 3.000&Aring;" /> '''The crystal struct...)
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[[Image:1zt4.gif|left|200px]]<br /><applet load="1zt4" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1zt4" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1zt4, resolution 3.000&Aring;" />
caption="1zt4, resolution 3.000&Aring;" />
'''The crystal structure of human CD1d with and without alpha-Galactosylceramide'''<br />
'''The crystal structure of human CD1d with and without alpha-Galactosylceramide'''<br />
==Overview==
==Overview==
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The glycolipid alpha-galactosylceramide binds with high affinity to CD1d, and stimulates natural killer T cells. Here we report the crystal, structure of human CD1d in complex with synthetic alpha-galactosylceramide, at a resolution of 3.0 A. The structure shows a tightly fit lipid in the, CD1d binding groove, with the sphingosine chain bound in the C' pocket and, the longer acyl chain anchored in the A' pocket. We also present the CD1d, structure without lipid, which has a more open conformation of the binding, groove, suggesting a dual conformation of CD1d in which the 'open', conformation is more able to load lipids. These structures provide clues, as to how CD1 molecules load glycolipids as well as data to guide the, design of new therapeutic agents.
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The glycolipid alpha-galactosylceramide binds with high affinity to CD1d and stimulates natural killer T cells. Here we report the crystal structure of human CD1d in complex with synthetic alpha-galactosylceramide at a resolution of 3.0 A. The structure shows a tightly fit lipid in the CD1d binding groove, with the sphingosine chain bound in the C' pocket and the longer acyl chain anchored in the A' pocket. We also present the CD1d structure without lipid, which has a more open conformation of the binding groove, suggesting a dual conformation of CD1d in which the 'open' conformation is more able to load lipids. These structures provide clues as to how CD1 molecules load glycolipids as well as data to guide the design of new therapeutic agents.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1ZT4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with AGH as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZT4 OCA].
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1ZT4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=AGH:'>AGH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZT4 OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Besra, G.S.]]
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[[Category: Besra, G S.]]
[[Category: Cerundolo, V.]]
[[Category: Cerundolo, V.]]
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[[Category: Fersht, A.R.]]
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[[Category: Fersht, A R.]]
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[[Category: Gadola, S.D.]]
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[[Category: Gadola, S D.]]
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[[Category: Jones, E.Y.]]
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[[Category: Jones, E Y.]]
[[Category: Koch, M.]]
[[Category: Koch, M.]]
[[Category: Mathew, B.]]
[[Category: Mathew, B.]]
[[Category: Ritter, G.]]
[[Category: Ritter, G.]]
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[[Category: SPINE, Structural.Proteomics.in.Europe.]]
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[[Category: SPINE, Structural Proteomics in Europe.]]
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[[Category: Schmidt, R.R.]]
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[[Category: Schmidt, R R.]]
[[Category: Shepherd, D.]]
[[Category: Shepherd, D.]]
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[[Category: Stronge, V.S.]]
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[[Category: Stronge, V S.]]
[[Category: AGH]]
[[Category: AGH]]
[[Category: alpha-galactosylceramide]]
[[Category: alpha-galactosylceramide]]
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[[Category: structural proteomics in europe]]
[[Category: structural proteomics in europe]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:40:59 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:18:51 2008''

Revision as of 14:18, 21 February 2008


1zt4, resolution 3.000Å

Drag the structure with the mouse to rotate

The crystal structure of human CD1d with and without alpha-Galactosylceramide

Contents

Overview

The glycolipid alpha-galactosylceramide binds with high affinity to CD1d and stimulates natural killer T cells. Here we report the crystal structure of human CD1d in complex with synthetic alpha-galactosylceramide at a resolution of 3.0 A. The structure shows a tightly fit lipid in the CD1d binding groove, with the sphingosine chain bound in the C' pocket and the longer acyl chain anchored in the A' pocket. We also present the CD1d structure without lipid, which has a more open conformation of the binding groove, suggesting a dual conformation of CD1d in which the 'open' conformation is more able to load lipids. These structures provide clues as to how CD1 molecules load glycolipids as well as data to guide the design of new therapeutic agents.

Disease

Known disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]

About this Structure

1ZT4 is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

The crystal structure of human CD1d with and without alpha-galactosylceramide., Koch M, Stronge VS, Shepherd D, Gadola SD, Mathew B, Ritter G, Fersht AR, Besra GS, Schmidt RR, Jones EY, Cerundolo V, Nat Immunol. 2005 Aug;6(8):819-26. Epub 2005 Jul 10. PMID:16007090

Page seeded by OCA on Thu Feb 21 16:18:51 2008

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