1i3r: Difference between revisions

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[[Image:1i3r.jpg|left|200px]]


{{Structure
==CRYSTAL STRUCTURE OF A MUTANT IEK CLASS II MHC MOLECULE==
|PDB= 1i3r |SIZE=350|CAPTION= <scene name='initialview01'>1i3r</scene>, resolution 2.4&Aring;
<StructureSection load='1i3r' size='340' side='right'caption='[[1i3r]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>
<table><tr><td colspan='2'>[[1i3r]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I3R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I3R 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]] 2.4&#8491;</td></tr>
|GENE= IEK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i3r OCA], [https://pdbe.org/1i3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i3r RCSB], [https://www.ebi.ac.uk/pdbsum/1i3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i3r ProSAT]</span></td></tr>
|RELATEDENTRY=[[1iea|1IEA]], [[1ieb|1IEB]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i3r OCA], [http://www.ebi.ac.uk/pdbsum/1i3r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i3r RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/HA22_MOUSE HA22_MOUSE]
 
== Evolutionary Conservation ==
'''CRYSTAL STRUCTURE OF A MUTANT IEK CLASS II MHC MOLECULE'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i3/1i3r_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=1i3r ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
IE/DR MHC class II molecules have an extensive H-bonding network under the bound peptide. In IE(k), two alpha chain acidic amino acids in the core of this network were mutated to amides. At low pH, the mutant molecule exchanged peptide much more rapidly than the wild-type. The crystal structure of the mutant IE(k) revealed the loss of a single buried water molecule and a reorganization of the predicted H-bonding network. We suggest that these mutations enhance the transition of MHC class II to an open conformation at low pH allowing the bound peptide to escape. In wild-type IE(k), the need to protonate these amino acids also may be a bottleneck in the return to a closed conformation after peptide binding.
IE/DR MHC class II molecules have an extensive H-bonding network under the bound peptide. In IE(k), two alpha chain acidic amino acids in the core of this network were mutated to amides. At low pH, the mutant molecule exchanged peptide much more rapidly than the wild-type. The crystal structure of the mutant IE(k) revealed the loss of a single buried water molecule and a reorganization of the predicted H-bonding network. We suggest that these mutations enhance the transition of MHC class II to an open conformation at low pH allowing the bound peptide to escape. In wild-type IE(k), the need to protonate these amino acids also may be a bottleneck in the return to a closed conformation after peptide binding.


==About this Structure==
Mutations changing the kinetics of class II MHC peptide exchange.,Wilson N, Fremont D, Marrack P, Kappler J Immunity. 2001 May;14(5):513-22. PMID:11371354<ref>PMID:11371354</ref>
1I3R 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=1I3R OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Mutations changing the kinetics of class II MHC peptide exchange., Wilson N, Fremont D, Marrack P, Kappler J, Immunity. 2001 May;14(5):513-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11371354 11371354]
</div>
<div class="pdbe-citations 1i3r" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Kappler JW]]
[[Category: Kappler, J W.]]
[[Category: Wilson N]]
[[Category: Wilson, N.]]
[[Category: mhc classii]]
[[Category: peptide]]
 
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