1oay

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<StructureSection load='1oay' size='340' side='right'caption='[[1oay]], [[Resolution|resolution]] 2.66&Aring;' scene=''>
<StructureSection load='1oay' size='340' side='right'caption='[[1oay]], [[Resolution|resolution]] 2.66&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1oay]] is a 6 chain structure with sequence from [https://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=1OAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OAY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1oay]] is a 6 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=1OAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OAY 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=FUR:FURAZOLIDONE'>FUR</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]] 2.66&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1oaq|1oaq]], [[1oau|1oau]], [[1oar|1oar]], [[1oax|1oax]], [[1oaz|1oaz]]</div></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=FUR:FURAZOLIDONE'>FUR</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oay OCA], [https://pdbe.org/1oay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oay RCSB], [https://www.ebi.ac.uk/pdbsum/1oay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oay ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oay OCA], [https://pdbe.org/1oay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oay RCSB], [https://www.ebi.ac.uk/pdbsum/1oay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oay ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LV1B_MOUSE LV1B_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=1oay 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=1oay 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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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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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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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 1oay" style="background-color:#fffaf0;"></div>
 
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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: James, L C]]
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[[Category: James LC]]
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[[Category: Roversi, P]]
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[[Category: Roversi P]]
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[[Category: Tawfik, D]]
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[[Category: Tawfik D]]
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[[Category: Allergy]]
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[[Category: Antibody]]
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[[Category: Antibody-complex]]
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[[Category: Conformational diversity]]
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[[Category: Ige]]
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[[Category: Immune system]]
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[[Category: Multispecificity]]
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Revision as of 05:45, 17 April 2024

Antibody multispecificity mediated by conformational diversity

PDB ID 1oay

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