1t0m
From Proteopedia
(New page: 200px<br /><applet load="1t0m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t0m, resolution 2.0Å" /> '''Conformational switch...) |
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| - | [[Image:1t0m.jpg|left|200px]]<br /><applet load="1t0m" size=" | + | [[Image:1t0m.jpg|left|200px]]<br /><applet load="1t0m" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1t0m, resolution 2.0Å" /> | caption="1t0m, resolution 2.0Å" /> | ||
'''Conformational switch in polymorphic H-2K molecules containing an HSV peptide'''<br /> | '''Conformational switch in polymorphic H-2K molecules containing an HSV peptide'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Polymorphism within the MHC not only affects peptide specificity but also | + | 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== | ==About this Structure== | ||
| - | 1T0M 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:// | + | 1T0M 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=1T0M OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Beddoe, T.]] | [[Category: Beddoe, T.]] | ||
| - | [[Category: Borg, N | + | [[Category: Borg, N A.]] |
| - | [[Category: Bottomley, S | + | [[Category: Bottomley, S P.]] |
| - | [[Category: Carbone, F | + | [[Category: Carbone, F R.]] |
| - | [[Category: Dunstone, M | + | [[Category: Dunstone, M A.]] |
[[Category: Kjer-Nielsen, L.]] | [[Category: Kjer-Nielsen, L.]] | ||
[[Category: McCluskey, J.]] | [[Category: McCluskey, J.]] | ||
| - | [[Category: Purcell, A | + | [[Category: Purcell, A W.]] |
[[Category: Rossjohn, J.]] | [[Category: Rossjohn, J.]] | ||
| - | [[Category: Webb, A | + | [[Category: Webb, A I.]] |
[[Category: hsv peptide]] | [[Category: hsv peptide]] | ||
[[Category: immunoglobulin domain]] | [[Category: immunoglobulin domain]] | ||
[[Category: mhc class i alpha domains]] | [[Category: mhc class i alpha domains]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:08:35 2008'' |
Revision as of 13:08, 21 February 2008
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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
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