1g6r

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(New page: 200px<br /><applet load="1g6r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g6r, resolution 2.8&Aring;" /> '''A FUNCTIONAL HOT SPOT...)
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[[Image:1g6r.gif|left|200px]]<br /><applet load="1g6r" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1g6r, resolution 2.8&Aring;" />
caption="1g6r, resolution 2.8&Aring;" />
'''A FUNCTIONAL HOT SPOT FOR ANTIGEN RECOGNITION IN A SUPERAGONIST TCR/MHC COMPLEX'''<br />
'''A FUNCTIONAL HOT SPOT FOR ANTIGEN RECOGNITION IN A SUPERAGONIST TCR/MHC COMPLEX'''<br />
==Overview==
==Overview==
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A longstanding question in T cell receptor signaling is how structurally, similar ligands, with similar affinities, can have substantially different, biological activity. The crystal structure of the 2C TCR complex of H-2Kb, with superagonist peptide SIYR at 2.8 A elucidates a structural basis for, TCR discrimination of altered peptide ligands. The difference in antigen, potency is modulated by two cavities in the TCR combining site, formed, mainly by CDRs 3alpha, 3beta, and 1beta, that complement centrally located, peptide residues. This "functional hot spot" allows the TCR to finely, discriminate amongst energetically similar interactions within different, ligands for those in which the peptide appropriately stabilizes the, TCR/pMHC complex and provides a new structural perspective for, understanding differential signaling resulting from T cell, cross-reactivity.
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A longstanding question in T cell receptor signaling is how structurally similar ligands, with similar affinities, can have substantially different biological activity. The crystal structure of the 2C TCR complex of H-2Kb with superagonist peptide SIYR at 2.8 A elucidates a structural basis for TCR discrimination of altered peptide ligands. The difference in antigen potency is modulated by two cavities in the TCR combining site, formed mainly by CDRs 3alpha, 3beta, and 1beta, that complement centrally located peptide residues. This "functional hot spot" allows the TCR to finely discriminate amongst energetically similar interactions within different ligands for those in which the peptide appropriately stabilizes the TCR/pMHC complex and provides a new structural perspective for understanding differential signaling resulting from T cell cross-reactivity.
==About this Structure==
==About this Structure==
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1G6R is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G6R OCA].
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1G6R is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G6R OCA].
==Reference==
==Reference==
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[[Category: Apostolopoulos, V.]]
[[Category: Apostolopoulos, V.]]
[[Category: Degano, M.]]
[[Category: Degano, M.]]
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[[Category: Garcia, K.C.]]
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[[Category: Garcia, K C.]]
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[[Category: Rudolph, M.G.]]
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[[Category: Rudolph, M G.]]
[[Category: Teyton, L.]]
[[Category: Teyton, L.]]
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[[Category: Wilson, I.A.]]
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[[Category: Wilson, I A.]]
[[Category: major histocompatibility complex]]
[[Category: major histocompatibility complex]]
[[Category: superagonist]]
[[Category: superagonist]]
[[Category: t cell antigen receptor]]
[[Category: t cell antigen receptor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:45:41 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:42 2008''

Revision as of 10:46, 21 February 2008


1g6r, resolution 2.8Å

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A FUNCTIONAL HOT SPOT FOR ANTIGEN RECOGNITION IN A SUPERAGONIST TCR/MHC COMPLEX

Overview

A longstanding question in T cell receptor signaling is how structurally similar ligands, with similar affinities, can have substantially different biological activity. The crystal structure of the 2C TCR complex of H-2Kb with superagonist peptide SIYR at 2.8 A elucidates a structural basis for TCR discrimination of altered peptide ligands. The difference in antigen potency is modulated by two cavities in the TCR combining site, formed mainly by CDRs 3alpha, 3beta, and 1beta, that complement centrally located peptide residues. This "functional hot spot" allows the TCR to finely discriminate amongst energetically similar interactions within different ligands for those in which the peptide appropriately stabilizes the TCR/pMHC complex and provides a new structural perspective for understanding differential signaling resulting from T cell cross-reactivity.

About this Structure

1G6R is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

A functional hot spot for antigen recognition in a superagonist TCR/MHC complex., Degano M, Garcia KC, Apostolopoulos V, Rudolph MG, Teyton L, Wilson IA, Immunity. 2000 Mar;12(3):251-61. PMID:10755612

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