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New page: left|200px<br /><applet load="1rjz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rjz, resolution 2.60Å" /> '''Mhc Class I Natural ...
 
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[[Image:1rjz.jpg|left|200px]]<br /><applet load="1rjz" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1rjz, resolution 2.60&Aring;" />
'''Mhc Class I Natural Mutant H-2Kbm8 Heavy Chain Complexed With beta-2 Microglobulin and Herpies Simplex Virus Mutant Glycoprotein B Peptide'''<br />


==Overview==
==Mhc Class I Natural Mutant H-2Kbm8 Heavy Chain Complexed With beta-2 Microglobulin and Herpies Simplex Virus Mutant Glycoprotein B Peptide==
Major histocompatibility complex (MHC) class I variants H-2K(b) and, H-2K(bm8) differ primarily in the B pocket of the peptide-binding groove, which serves to sequester the P2 secondary anchor residue. This, polymorphism determines resistance to lethal herpes simplex virus (HSV-1), infection by modulating T cell responses to the immunodominant, glycoprotein B(498-505) epitope, HSV8. We studied the molecular basis of, these effects and confirmed that T cell receptors raised against K(b)-HSV8, cannot recognize H-2K(bm8)-HSV8. However, substitution of Ser(P2) to, Glu(P2) (peptide H2E) reversed T cell receptor (TCR) recognition;, H-2K(bm8)-H2E was recognized whereas H-2K(b)-H2E was not. Insight into the, structural basis of this discrimination was obtained by determining the, crystal structures of all four MHC class I molecules in complex with bound, peptide (pMHCs). Surprisingly, we find no concerted pMHC surface, differences that can explain the differential TCR recognition. However, a, correlation is apparent between the recognition data and the underlying, peptide-binding groove chemistry of the B pocket, revealing that secondary, anchor residues can profoundly affect TCR engagement through mechanisms, distinct from the alteration of the resting state conformation of the pMHC, surface.
<StructureSection load='1rjz' size='340' side='right'caption='[[1rjz]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1rjz]] 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=1RJZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RJZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#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=1rjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rjz OCA], [https://pdbe.org/1rjz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rjz RCSB], [https://www.ebi.ac.uk/pdbsum/1rjz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rjz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HA1B_MOUSE HA1B_MOUSE] Involved in the presentation of foreign antigens to the immune system.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rj/1rjz_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1rjz ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1RJZ 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RJZ OCA].
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
 
*[[MHC 3D structures|MHC 3D structures]]
==Reference==
*[[MHC I 3D structures|MHC I 3D structures]]
Structural basis for the restoration of TCR recognition of an MHC allelic variant by peptide secondary anchor substitution., Miley MJ, Messaoudi I, Metzner BM, Wu Y, Nikolich-Zugich J, Fremont DH, J Exp Med. 2004 Dec 6;200(11):1445-54. Epub 2004 Nov 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15557346 15557346]
__TOC__
</StructureSection>
[[Category: Human alphaherpesvirus 1 strain F]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Fremont DH]]
[[Category: Fremont, D.H.]]
[[Category: Messaoudi I]]
[[Category: Messaoudi, I.]]
[[Category: Miley MJ]]
[[Category: Miley, M.J.]]
[[Category: Nikolich-Zugich J]]
[[Category: Nikolich-Zugich, J.]]
[[Category: class i]]
[[Category: herpes]]
[[Category: mhc]]
[[Category: peptide]]
[[Category: tcr]]
[[Category: virus]]
 
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