1kgc

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(New page: 200px<br /> <applet load="1kgc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kgc, resolution 1.5&Aring;" /> '''Immune Receptor'''<b...)
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<applet load="1kgc" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1kgc, resolution 1.5&Aring;" />
'''Immune Receptor'''<br />
'''Immune Receptor'''<br />
==Overview==
==Overview==
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Despite a potential repertoire of &gt;10(15) alphabeta T cell receptors, (TcR), the HLA B8-restricted cytolytic T cell response to a latent antigen, of Epstein-Barr virus (EBV) is strikingly limited in the TcR sequences, that are selected. Even in unrelated individuals this response is, dominated by a single highly restricted TcR clonotype that selects, identical combinations of hypervariable Valpha, Vbeta, D, J, and N region, genes. We have determined the 1.5 A crystal structure of this "public", TcR, revealing that five of the six hypervariable loops adopt novel, conformations providing a unique combining site that contains a deep, pocket predicted to overlay the HLA B8-peptide complex. The findings, suggest a structural basis for the immunodominance of this clonotype in, the immune response to EBV.
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Despite a potential repertoire of &gt;10(15) alphabeta T cell receptors (TcR), the HLA B8-restricted cytolytic T cell response to a latent antigen of Epstein-Barr virus (EBV) is strikingly limited in the TcR sequences that are selected. Even in unrelated individuals this response is dominated by a single highly restricted TcR clonotype that selects identical combinations of hypervariable Valpha, Vbeta, D, J, and N region genes. We have determined the 1.5 A crystal structure of this "public" TcR, revealing that five of the six hypervariable loops adopt novel conformations providing a unique combining site that contains a deep pocket predicted to overlay the HLA B8-peptide complex. The findings suggest a structural basis for the immunodominance of this clonotype in the immune response to EBV.
==About this Structure==
==About this Structure==
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1KGC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KGC OCA].
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1KGC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1KGC OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Brooks, A.G.]]
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[[Category: Brooks, A G.]]
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[[Category: Clements, C.S.]]
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[[Category: Clements, C S.]]
[[Category: Kjer-Nielsen, L.]]
[[Category: Kjer-Nielsen, L.]]
[[Category: McCluskey, J.]]
[[Category: McCluskey, J.]]
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[[Category: Purcell, A.W.]]
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[[Category: Purcell, A W.]]
[[Category: Rossjohn, J.]]
[[Category: Rossjohn, J.]]
[[Category: lc13 clone]]
[[Category: lc13 clone]]
[[Category: t-cell receptor]]
[[Category: t-cell receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:50:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:49 2008''

Revision as of 11:33, 21 February 2008


1kgc, resolution 1.5Å

Drag the structure with the mouse to rotate

Immune Receptor

Overview

Despite a potential repertoire of >10(15) alphabeta T cell receptors (TcR), the HLA B8-restricted cytolytic T cell response to a latent antigen of Epstein-Barr virus (EBV) is strikingly limited in the TcR sequences that are selected. Even in unrelated individuals this response is dominated by a single highly restricted TcR clonotype that selects identical combinations of hypervariable Valpha, Vbeta, D, J, and N region genes. We have determined the 1.5 A crystal structure of this "public" TcR, revealing that five of the six hypervariable loops adopt novel conformations providing a unique combining site that contains a deep pocket predicted to overlay the HLA B8-peptide complex. The findings suggest a structural basis for the immunodominance of this clonotype in the immune response to EBV.

About this Structure

1KGC is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The 1.5 A crystal structure of a highly selected antiviral T cell receptor provides evidence for a structural basis of immunodominance., Kjer-Nielsen L, Clements CS, Brooks AG, Purcell AW, McCluskey J, Rossjohn J, Structure. 2002 Nov;10(11):1521-32. PMID:12429093

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