1oau

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[[Image:1oau.jpg|left|200px]]<br /><applet load="1oau" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1oau, resolution 1.8&Aring;" />
 
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'''FV STRUCTURE OF THE IGE SPE-7 IN COMPLEX WITH DNP-SER (IMMUNISING HAPTEN)'''<br />
 
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==Overview==
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==Fv Structure of the IgE SPE-7 in complex with DNP-Ser (immunising hapten)==
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A single antibody was shown to adopt different binding-site conformations, and thereby bind unrelated antigens. Analysis by both x-ray, crystallography and pre-steady-state kinetics revealed an equilibrium, between different preexisting isomers, one of which possessed a, promiscuous, low-affinity binding site for aromatic ligands, including the, immunizing hapten. A subsequent induced-fit isomerization led to, high-affinity complexes with a deep and narrow binding site. A protein, antigen identified by repertoire selection made use of an unrelated, antibody isomer with a wide, shallow binding site. Conformational, diversity, whereby one sequence adopts multiple structures and multiple, functions, can increase the effective size of the antibody repertoire but, may also lead to autoimmunity and allergy.
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<StructureSection load='1oau' size='340' side='right'caption='[[1oau]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1oau]] 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=1OAU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OAU FirstGlance]. <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]] 1.8&#8491;</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=DNF:2,4-DINITROPHENOL'>DNF</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=SER:SERINE'>SER</scene></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=1oau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oau OCA], [https://pdbe.org/1oau PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oau RCSB], [https://www.ebi.ac.uk/pdbsum/1oau PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oau ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LV1B_MOUSE LV1B_MOUSE]
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== Evolutionary Conservation ==
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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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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oa/1oau_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1oau 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 ==
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A single antibody was shown to adopt different binding-site conformations and thereby bind unrelated antigens. Analysis by both x-ray crystallography and pre-steady-state kinetics revealed an equilibrium between different preexisting isomers, one of which possessed a promiscuous, low-affinity binding site for aromatic ligands, including the immunizing hapten. A subsequent induced-fit isomerization led to high-affinity complexes with a deep and narrow binding site. A protein antigen identified by repertoire selection made use of an unrelated antibody isomer with a wide, shallow binding site. Conformational diversity, whereby one sequence adopts multiple structures and multiple functions, can increase the effective size of the antibody repertoire but may also lead to autoimmunity and allergy.
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==About this Structure==
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Antibody multispecificity mediated by conformational diversity.,James LC, Roversi P, Tawfik DS Science. 2003 Feb 28;299(5611):1362-7. PMID:12610298<ref>PMID:12610298</ref>
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1OAU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] with <scene name='pdbligand=SER:'>SER</scene> and <scene name='pdbligand=IMD:'>IMD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Imd+Binding+Site+For+Chain+N'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OAU 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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Antibody multispecificity mediated by conformational diversity., James LC, Roversi P, Tawfik DS, Science. 2003 Feb 28;299(5611):1362-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12610298 12610298]
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</div>
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[[Category: Rattus rattus]]
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<div class="pdbe-citations 1oau" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: James, L.C.]]
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<references/>
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[[Category: Roversi, P.]]
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__TOC__
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[[Category: Tawfik, D.]]
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</StructureSection>
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[[Category: IMD]]
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[[Category: Large Structures]]
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[[Category: SER]]
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[[Category: Mus musculus]]
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[[Category: allergy]]
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[[Category: James LC]]
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[[Category: antibody]]
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[[Category: Roversi P]]
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[[Category: conformational diversity]]
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[[Category: Tawfik D]]
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[[Category: ige]]
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[[Category: multispecificity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:55:41 2008''
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Current revision

Fv Structure of the IgE SPE-7 in complex with DNP-Ser (immunising hapten)

PDB ID 1oau

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