1s7q: Difference between revisions

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[[Image:1s7q.gif|left|200px]]


{{Structure
==Crystal structures of the murine class I major histocompatibility complex H-2Kb in complex with LCMV-derived gp33 index peptide and three of its escape variants==
|PDB= 1s7q |SIZE=350|CAPTION= <scene name='initialview01'>1s7q</scene>, resolution 1.99&Aring;
<StructureSection load='1s7q' size='340' side='right'caption='[[1s7q]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1s7q]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Lymphocytic_choriomeningitis_virus_(strain_WE) Lymphocytic choriomeningitis virus (strain WE)] 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=1S7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S7Q FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.99&#8491;</td></tr>
|GENE= H2-K ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), B2M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1s7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s7q OCA], [https://pdbe.org/1s7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s7q RCSB], [https://www.ebi.ac.uk/pdbsum/1s7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s7q ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=[[1n59|1N59]], [[1s7r|1S7R]], [[1s7s|1S7S]], [[1s7t|1S7T]], [[1s7u|1S7U]], [[1s7v|1S7V]], [[1s7w|1S7W]], [[1s7x|1S7X]]
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s7q OCA], [http://www.ebi.ac.uk/pdbsum/1s7q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s7q RCSB]</span>
[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/s7/1s7q_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1s7q ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lymphocytic choriomeningitis virus infection of H-2(b) mice generates a strong CD8(+) CTL response mainly directed toward three immunodominant epitopes, one of which, gp33, is presented by both H-2D(b) and H-2K(b) MHC class I molecules. This CTL response acts as a selective agent for the emergence of viral escape variants. These variants generate altered peptide ligands (APLs) that, when presented by class I MHC molecules, antagonize CTL recognition and ultimately allow the virus to evade the cellular immune response. The emergence of APLs of the gp33 epitope is particularly advantageous for LCMV, as it allows viral escape in the context of both H-2D(b) and H-2K(b) MHC class I molecules. We have determined crystal structures of three different APLs of gp33 in complex with both H-2D(b) and H-2K(b). Comparison between these APL/MHC structures and those of the index gp33 peptide/MHC reveals the structural basis for three different strategies used by LCMV viral escape mutations: 1) conformational changes in peptide and MHC residues that are potential TCR contacts, 2) impairment of APL binding to the MHC peptide binding cleft, and 3) introduction of subtle changes at the TCR/pMHC interface, such as the removal of a single hydroxyl group.


'''Crystal structures of the murine class I major histocompatibility complex H-2Kb in complex with LCMV-derived gp33 index peptide and three of its escape variants'''
Determination of structural principles underlying three different modes of lymphocytic choriomeningitis virus escape from CTL recognition.,Velloso LM, Michaelsson J, Ljunggren HG, Schneider G, Achour A J Immunol. 2004 May 1;172(9):5504-11. PMID:15100292<ref>PMID:15100292</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1s7q" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Lymphocytic choriomeningitis virus infection of H-2(b) mice generates a strong CD8(+) CTL response mainly directed toward three immunodominant epitopes, one of which, gp33, is presented by both H-2D(b) and H-2K(b) MHC class I molecules. This CTL response acts as a selective agent for the emergence of viral escape variants. These variants generate altered peptide ligands (APLs) that, when presented by class I MHC molecules, antagonize CTL recognition and ultimately allow the virus to evade the cellular immune response. The emergence of APLs of the gp33 epitope is particularly advantageous for LCMV, as it allows viral escape in the context of both H-2D(b) and H-2K(b) MHC class I molecules. We have determined crystal structures of three different APLs of gp33 in complex with both H-2D(b) and H-2K(b). Comparison between these APL/MHC structures and those of the index gp33 peptide/MHC reveals the structural basis for three different strategies used by LCMV viral escape mutations: 1) conformational changes in peptide and MHC residues that are potential TCR contacts, 2) impairment of APL binding to the MHC peptide binding cleft, and 3) introduction of subtle changes at the TCR/pMHC interface, such as the removal of a single hydroxyl group.
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
 
*[[MHC 3D structures|MHC 3D structures]]
==About this Structure==
*[[MHC I 3D structures|MHC I 3D structures]]
1S7Q 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=1S7Q OCA].
== References ==
 
<references/>
==Reference==
__TOC__
Determination of structural principles underlying three different modes of lymphocytic choriomeningitis virus escape from CTL recognition., Velloso LM, Michaelsson J, Ljunggren HG, Schneider G, Achour A, J Immunol. 2004 May 1;172(9):5504-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15100292 15100292]
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Achour A]]
[[Category: Achour, A.]]
[[Category: Ljunggren HG]]
[[Category: Ljunggren, H G.]]
[[Category: Michaelsson J]]
[[Category: Michaelsson, J.]]
[[Category: Schneider G]]
[[Category: Schneider, G.]]
[[Category: Velloso LM]]
[[Category: Velloso, L M.]]
[[Category: immune escape]]
[[Category: lcmv]]
[[Category: mhc class i]]
 
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