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1i3r

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<StructureSection load='1i3r' size='340' side='right'caption='[[1i3r]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1i3r' size='340' side='right'caption='[[1i3r]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1i3r]] is a 8 chain structure with sequence from [http://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=1I3R OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1I3R FirstGlance]. <br>
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<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>
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</td></tr><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>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1iea|1iea]], [[1ieb|1ieb]]</td></tr>
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<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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IEK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1i3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i3r OCA], [http://pdbe.org/1i3r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i3r RCSB], [http://www.ebi.ac.uk/pdbsum/1i3r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1i3r ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/HBB2_MOUSE HBB2_MOUSE]] Involved in oxygen transport from the lung to the various peripheral tissues.
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[https://www.uniprot.org/uniprot/HA22_MOUSE HA22_MOUSE]
== 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=1i3r 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=1i3r ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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.
 
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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>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1i3r" style="background-color:#fffaf0;"></div>
 
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==See Also==
 
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*[[MHC 3D structures|MHC 3D structures]]
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lk3 transgenic mice]]
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[[Category: Mus musculus]]
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[[Category: Kappler, J W]]
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[[Category: Kappler JW]]
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[[Category: Wilson, N]]
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[[Category: Wilson N]]
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[[Category: Immune system]]
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[[Category: Mhc classii]]
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Current revision

CRYSTAL STRUCTURE OF A MUTANT IEK CLASS II MHC MOLECULE

PDB ID 1i3r

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