1kgc: Difference between revisions

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New page: left|200px<br /> <applet load="1kgc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kgc, resolution 1.5Å" /> '''Immune Receptor'''<b...
 
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[[Image:1kgc.gif|left|200px]]<br />
[[Image:1kgc.gif|left|200px]]<br /><applet load="1kgc" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1kgc" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1kgc, resolution 1.5&Aring;" />
caption="1kgc, resolution 1.5&Aring;" />
'''Immune Receptor'''<br />
'''Immune Receptor'''<br />


==Overview==
==Overview==
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.
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==
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].  
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]]
[[Category: Brooks, A.G.]]
[[Category: Brooks, A G.]]
[[Category: Clements, C.S.]]
[[Category: Clements, C S.]]
[[Category: Kjer-Nielsen, L.]]
[[Category: Kjer-Nielsen, L.]]
[[Category: McCluskey, J.]]
[[Category: McCluskey, J.]]
[[Category: Purcell, A.W.]]
[[Category: Purcell, A W.]]
[[Category: Rossjohn, J.]]
[[Category: Rossjohn, J.]]
[[Category: lc13 clone]]
[[Category: lc13 clone]]
[[Category: t-cell receptor]]
[[Category: t-cell receptor]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:50:42 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:49 2008''

Revision as of 14:33, 21 February 2008

File:1kgc.gif


1kgc, resolution 1.5Å

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Immune Receptor

OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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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