2wqr

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==THE HIGH RESOLUTION CRYSTAL STRUCTURE OF IGE FC==
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<StructureSection load='2wqr' size='340' side='right' caption='[[2wqr]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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==The high resolution crystal structure of IgE Fc==
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<StructureSection load='2wqr' size='340' side='right'caption='[[2wqr]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2wqr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WQR OCA]. <br>
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<table><tr><td colspan='2'>[[2wqr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WQR FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>
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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]] 1.9&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fp5|1fp5]], [[1g84|1g84]], [[1f6a|1f6a]], [[1ige|1ige]], [[1o0v|1o0v]]</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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></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=2wqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wqr OCA], [https://pdbe.org/2wqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wqr RCSB], [https://www.ebi.ac.uk/pdbsum/2wqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wqr ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wqr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wqr RCSB], [http://www.ebi.ac.uk/pdbsum/2wqr PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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[https://www.uniprot.org/uniprot/IGHE_HUMAN IGHE_HUMAN]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcvarepsilonRI.,Holdom MD, Davies AM, Nettleship JE, Bagby SC, Dhaliwal B, Girardi E, Hunt J, Gould HJ, Beavil AJ, McDonnell JM, Owens RJ, Sutton BJ Nat Struct Mol Biol. 2011 May;18(5):571-6. Epub 2011 Apr 24. PMID:21516097<ref>PMID:21516097</ref>
Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcvarepsilonRI.,Holdom MD, Davies AM, Nettleship JE, Bagby SC, Dhaliwal B, Girardi E, Hunt J, Gould HJ, Beavil AJ, McDonnell JM, Owens RJ, Sutton BJ Nat Struct Mol Biol. 2011 May;18(5):571-6. Epub 2011 Apr 24. PMID:21516097<ref>PMID:21516097</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 2wqr" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Beavil, A J.]]
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[[Category: Large Structures]]
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[[Category: Dhaliwal, B.]]
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[[Category: Beavil AJ]]
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[[Category: Sutton, B J.]]
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[[Category: Dhaliwal B]]
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[[Category: Glycoprotein]]
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[[Category: Sutton BJ]]
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[[Category: Immune system]]
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[[Category: Immunoglobulin domain]]
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Current revision

The high resolution crystal structure of IgE Fc

PDB ID 2wqr

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