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1t0m

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[[Image:1t0m.jpg|left|200px]]
[[Image:1t0m.jpg|left|200px]]
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{{Structure
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|RELATEDENTRY=[[1t0n|1T0N]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t0m OCA], [http://www.ebi.ac.uk/pdbsum/1t0m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t0m RCSB]</span>
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'''Conformational switch in polymorphic H-2K molecules containing an HSV peptide'''
'''Conformational switch in polymorphic H-2K molecules containing an HSV peptide'''
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[[Category: Rossjohn, J.]]
[[Category: Rossjohn, J.]]
[[Category: Webb, A I.]]
[[Category: Webb, A I.]]
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[[Category: hsv peptide]]
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[[Category: Hsv peptide]]
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[[Category: immunoglobulin domain]]
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[[Category: Immunoglobulin domain]]
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[[Category: mhc class i alpha domain]]
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[[Category: Mhc class i alpha domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:21:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:49:32 2008''
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Revision as of 06:21, 3 May 2008

Template:STRUCTURE 1t0m

Conformational switch in polymorphic H-2K molecules containing an HSV peptide


Overview

Polymorphism within the MHC not only affects peptide specificity but also has a critical influence on the T cell repertoire; for example, the CD8 T cell response toward an immunodominant HSV glycoprotein B peptide is more diverse and of higher avidity in H-2(bm8) compared with H-2(b) mice. We have examined the basis for the selection of these distinct antiviral T cell repertoires by comparing the high-resolution structures of K(b) and K(bm8), in complex with cognate peptide Ag. Although K(b) and K(bm8) differ by four residues within the Ag-binding cleft, the most striking difference in the two structures was the disparate conformation adopted by the shared residue, Arg(62). The altered dynamics of Arg(62), coupled with a small rigid-body movement in the alpha(1) helix encompassing this residue, correlated with biased Valpha usage in the B6 mice. Moreover, an analysis of all known TCR/MHC complexes reveals that Arg(62) invariably interacts with the TCR CDR1alpha loop. Accordingly, Arg(62) appears to function as a conformational switch that may govern T cell selection and protective immunity.

About this Structure

1T0M is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

The structure of H-2K(b) and K(bm8) complexed to a herpes simplex virus determinant: evidence for a conformational switch that governs T cell repertoire selection and viral resistance., Webb AI, Borg NA, Dunstone MA, Kjer-Nielsen L, Beddoe T, McCluskey J, Carbone FR, Bottomley SP, Aguilar MI, Purcell AW, Rossjohn J, J Immunol. 2004 Jul 1;173(1):402-9. PMID:15210799 Page seeded by OCA on Sat May 3 09:21:26 2008

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