1t0m: Difference between revisions

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<StructureSection load='1t0m' size='340' side='right'caption='[[1t0m]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1t0m' size='340' side='right'caption='[[1t0m]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1t0m]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1T0M FirstGlance]. <br>
<table><tr><td colspan='2'>[[1t0m]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1_strain_F Human alphaherpesvirus 1 strain F] and [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1T0M FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1t0n|1t0n]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t0m OCA], [https://pdbe.org/1t0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t0m RCSB], [https://www.ebi.ac.uk/pdbsum/1t0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t0m ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t0m OCA], [https://pdbe.org/1t0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t0m RCSB], [https://www.ebi.ac.uk/pdbsum/1t0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t0m ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/HA1B_MOUSE HA1B_MOUSE]] Involved in the presentation of foreign antigens to the immune system. [[https://www.uniprot.org/uniprot/GB_HHV1F GB_HHV1F]] Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moities of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding of gD to one of its receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress. Also plays a role, together with gK, in virus-induced cell-to-cell fusion (syncytia formation) (By similarity).<ref>PMID:17548810</ref>  [[https://www.uniprot.org/uniprot/B2MG_MOUSE B2MG_MOUSE]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.  
[https://www.uniprot.org/uniprot/HA1B_MOUSE HA1B_MOUSE] Involved in the presentation of foreign antigens to the immune system.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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/main_output.php?pdb_ID=1t0m ConSurf].
</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/main_output.php?pdb_ID=1t0m ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<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>
</div>
<div class="pdbe-citations 1t0m" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
*[[MHC 3D structures|MHC 3D structures]]
*[[MHC 3D structures|MHC 3D structures]]
== References ==
*[[MHC I 3D structures|MHC I 3D structures]]
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human alphaherpesvirus 1 strain F]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Mus musculus]]
[[Category: Beddoe, T]]
[[Category: Beddoe T]]
[[Category: Borg, N A]]
[[Category: Borg NA]]
[[Category: Bottomley, S P]]
[[Category: Bottomley SP]]
[[Category: Carbone, F R]]
[[Category: Carbone FR]]
[[Category: Dunstone, M A]]
[[Category: Dunstone MA]]
[[Category: Kjer-Nielsen, L]]
[[Category: Kjer-Nielsen L]]
[[Category: McCluskey, J]]
[[Category: McCluskey J]]
[[Category: Purcell, A W]]
[[Category: Purcell AW]]
[[Category: Rossjohn, J]]
[[Category: Rossjohn J]]
[[Category: Webb, A I]]
[[Category: Webb AI]]
[[Category: Hsv peptide]]
[[Category: Immune system]]
[[Category: Immunoglobulin domain]]
[[Category: Mhc class i alpha domain]]

Latest revision as of 08:37, 1 May 2024

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

1t0m, resolution 2.00Å

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