1t0m

<StructureSection load='1t0m' size='340' side='right' caption='[[1t0m]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[1t0m]] is a 6 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T0M FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1t0n|1t0n]]</td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1t0m RCSB], [http://www.ebi.ac.uk/pdbsum/1t0m PDBsum]</span></td></tr>

<table>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t0/1t0m_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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<ref>PMID:15210799</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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*[[Beta-2 microglobulin|Beta-2 microglobulin]]

*[[Major histocompatibility complex|Major histocompatibility complex]]

[[Category: Beddoe, T.]]

[[Category: Borg, N A.]]

[[Category: Bottomley, S P.]]

[[Category: Carbone, F R.]]

[[Category: Dunstone, M A.]]

[[Category: Kjer-Nielsen, L.]]

[[Category: McCluskey, J.]]

[[Category: Purcell, A W.]]

[[Category: Rossjohn, J.]]

[[Category: Webb, A I.]]

[[Category: Mhc class i alpha domain]]