3mbe: Difference between revisions

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{{STRUCTURE_3mbe|  PDB=3mbe  |  SCENE=  }}
==TCR 21.30 in complex with MHC class II I-Ag7HEL(11-27)==
===TCR 21.30 in complex with MHC class II I-Ag7HEL(11-27)===
<StructureSection load='3mbe' size='340' side='right' caption='[[3mbe]], [[Resolution|resolution]] 2.89&Aring;' scene=''>
{{ABSTRACT_PUBMED_20407212}}
== Structural highlights ==
<table><tr><td colspan='2'>[[3mbe]] is a 10 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=3MBE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MBE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">H2-Aa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), H2-Ab1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mbe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mbe RCSB], [http://www.ebi.ac.uk/pdbsum/3mbe PDBsum]</span></td></tr>
</table>
== 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/mb/3mbe_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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Genetic susceptibility to autoimmunity is frequently associated with specific MHC alleles. Diabetogenic MHC class II molecules, such as human HLA-DQ8 and mouse I-Ag7, typically have a small, uncharged amino acid residue at position 57 of their beta chain (beta57); this results in the absence of a salt bridge between beta57 and Argalpha76, which is adjacent to the P9 pocket of the peptide-binding groove. However, the influence of Argalpha76 on the selection of the TCR repertoire remains unknown, particularly when the MHC molecule binds a peptide with a neutral amino acid residue at position P9. Here, we have shown that diabetogenic MHC class II molecules bound to a peptide with a neutral P9 residue primarily selected and expanded cells expressing TCRs bearing a negatively charged residue in the first segment of their complementarity determining region 3beta. The crystal structure of one such TCR in complex with I-Ag7 bound to a peptide containing a neutral P9 residue revealed that a network of favorable long-range (greater than 4 A) electrostatic interactions existed among Argalpha76, the neutral P9 residue, and TCR, which supported the substantially increased TCR/peptide-MHC affinity. This network could be modulated or switched to a lower affinity interaction by the introduction of a negative charge at position P9 of the peptide. Our results support the existence of a switch at residue beta57 of the I-Ag7 and HLA-DQ8 class II molecules and potentially link normal thymic TCR selection with abnormal peripheral behavior.


==Function==
The diabetogenic mouse MHC class II molecule I-Ag7 is endowed with a switch that modulates TCR affinity.,Yoshida K, Corper AL, Herro R, Jabri B, Wilson IA, Teyton L J Clin Invest. 2010 May 3;120(5):1578-90. doi: 10.1172/JCI41502. Epub 2010, Apr 19. PMID:20407212<ref>PMID:20407212</ref>
[[http://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK]] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref>


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[3mbe]] is a 10 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=3MBE OCA].
</div>


==See Also==
==See Also==
*[[Major histocompatibility complex|Major histocompatibility complex]]
*[[Major histocompatibility complex|Major histocompatibility complex]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:020407212</ref><references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Corper, A L.]]
[[Category: Corper, A L]]
[[Category: I A., Wilson.]]
[[Category: I A., Wilson]]
[[Category: Teyton, L.]]
[[Category: Teyton, L]]
[[Category: Yoshida, K.]]
[[Category: Yoshida, K]]
[[Category: Histocompatability antigen]]
[[Category: Histocompatability antigen]]
[[Category: I-ag7]]
[[Category: I-ag7]]
Retrieved from "https://proteopedia.org/3mbe"