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1t0m
From Proteopedia
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| - | [[Image:1t0m.jpg|left|200px]] | + | [[Image:1t0m.jpg|left|200px]] |
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| - | '''Conformational switch in polymorphic H-2K molecules containing an HSV peptide''' | + | {{Structure |
| + | |PDB= 1t0m |SIZE=350|CAPTION= <scene name='initialview01'>1t0m</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Conformational switch in polymorphic H-2K molecules containing an HSV peptide''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1T0M is a [ | + | 1T0M is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15210799 15210799] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: hsv peptide]] | [[Category: hsv peptide]] | ||
[[Category: immunoglobulin domain]] | [[Category: immunoglobulin domain]] | ||
| - | [[Category: mhc class i alpha | + | [[Category: mhc class i alpha domain]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:12:07 2008'' |
Revision as of 12:12, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 14:12:07 2008
