1o0v

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[[Image:1o0v.jpg|left|200px]]
 
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{{Structure
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==The crystal structure of IgE Fc reveals an asymmetrically bent conformation==
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|PDB= 1o0v |SIZE=350|CAPTION= <scene name='initialview01'>1o0v</scene>, resolution 2.6&Aring;
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<StructureSection load='1o0v' size='340' side='right'caption='[[1o0v]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <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=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1o0v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ls0 1ls0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O0V FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.6&#8491;</td></tr>
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|GENE= IgE(ND) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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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=1o0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o0v OCA], [https://pdbe.org/1o0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o0v RCSB], [https://www.ebi.ac.uk/pdbsum/1o0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o0v ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o0v OCA], [http://www.ebi.ac.uk/pdbsum/1o0v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o0v RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/IGHE_HUMAN IGHE_HUMAN]
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== Evolutionary Conservation ==
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'''The crystal structure of IgE Fc reveals an asymmetrically bent conformation'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o0/1o0v_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1o0v ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
The distinguishing structural feature of immunoglobulin E (IgE), the antibody responsible for allergic hypersensitivity, is the C epsilon 2 domain pair that replaces the hinge region of IgG. The crystal structure of the IgE Fc (constant fragment) at a 2.6-A resolution has revealed these domains. They display a distinctive, disulfide-linked Ig domain interface and are folded back asymmetrically onto the C epsilon 3 and C epsilon 4 domains, which causes an acute bend in the IgE molecule. The structure implies that a substantial conformational change involving C epsilon 2 must accompany binding to the mast cell receptor Fc epsilon RI. This may be the basis of the exceptionally slow dissociation rate of the IgE-Fc epsilon RI complex and, thus, of the ability of IgE to cause persistent allergic sensitization of mast cells.
The distinguishing structural feature of immunoglobulin E (IgE), the antibody responsible for allergic hypersensitivity, is the C epsilon 2 domain pair that replaces the hinge region of IgG. The crystal structure of the IgE Fc (constant fragment) at a 2.6-A resolution has revealed these domains. They display a distinctive, disulfide-linked Ig domain interface and are folded back asymmetrically onto the C epsilon 3 and C epsilon 4 domains, which causes an acute bend in the IgE molecule. The structure implies that a substantial conformational change involving C epsilon 2 must accompany binding to the mast cell receptor Fc epsilon RI. This may be the basis of the exceptionally slow dissociation rate of the IgE-Fc epsilon RI complex and, thus, of the ability of IgE to cause persistent allergic sensitization of mast cells.
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==About this Structure==
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The crystal structure of IgE Fc reveals an asymmetrically bent conformation.,Wan T, Beavil RL, Fabiane SM, Beavil AJ, Sohi MK, Keown M, Young RJ, Henry AJ, Owens RJ, Gould HJ, Sutton BJ Nat Immunol. 2002 Jul;3(7):681-6. Epub 2002 Jun 17. PMID:12068291<ref>PMID:12068291</ref>
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1O0V is a [[Single protein]] structure of 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=1O0V OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The crystal structure of IgE Fc reveals an asymmetrically bent conformation., Wan T, Beavil RL, Fabiane SM, Beavil AJ, Sohi MK, Keown M, Young RJ, Henry AJ, Owens RJ, Gould HJ, Sutton BJ, Nat Immunol. 2002 Jul;3(7):681-6. Epub 2002 Jun 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12068291 12068291]
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</div>
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<div class="pdbe-citations 1o0v" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Beavil, A J.]]
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[[Category: Beavil AJ]]
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[[Category: Beavil, R L.]]
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[[Category: Beavil RL]]
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[[Category: Fabiane, S M.]]
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[[Category: Fabiane SM]]
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[[Category: Gould, H J.]]
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[[Category: Gould HJ]]
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[[Category: Henry, A J.]]
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[[Category: Henry AJ]]
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[[Category: Keown, M.]]
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[[Category: Keown M]]
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[[Category: Owens, R J.]]
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[[Category: Owens RJ]]
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[[Category: Sohi, M K.]]
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[[Category: Sohi MK]]
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[[Category: Sutton, B J.]]
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[[Category: Sutton BJ]]
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[[Category: Wan, T.]]
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[[Category: Wan T]]
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[[Category: Young, R J.]]
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[[Category: Young RJ]]
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[[Category: ige fc]]
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[[Category: immunoglobulin e]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:38:17 2008''
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Current revision

The crystal structure of IgE Fc reveals an asymmetrically bent conformation

PDB ID 1o0v

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