1oaz: Difference between revisions

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[[Image:1oaz.jpg|left|200px]]
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{{STRUCTURE_1oaz|  PDB=1oaz  |  SCENE=  }}
'''IGE FV SPE7 COMPLEXED WITH A RECOMBINANT THIOREDOXIN'''


==IgE Fv SPE7 complexed with a recombinant thioredoxin==
<StructureSection load='1oaz' size='340' side='right'caption='[[1oaz]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1oaz]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OAZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.78&#8491;</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=1oaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oaz OCA], [https://pdbe.org/1oaz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oaz RCSB], [https://www.ebi.ac.uk/pdbsum/1oaz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oaz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/THIO_ECOLI THIO_ECOLI] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oa/1oaz_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1oaz ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1OAZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OAZ OCA].
</div>
<div class="pdbe-citations 1oaz" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Antibody multispecificity mediated by conformational diversity., James LC, Roversi P, Tawfik DS, Science. 2003 Feb 28;299(5611):1362-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12610298 12610298]
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Rattus rattus]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Mus musculus]]
[[Category: James, L C.]]
[[Category: James LC]]
[[Category: Roversi, P.]]
[[Category: Roversi P]]
[[Category: Tawfik, D.]]
[[Category: Tawfik D]]
[[Category: Allergy]]
[[Category: Antibody]]
[[Category: Conformational diversity]]
[[Category: Ige]]
[[Category: Multispecficity,redox-active center,electron transport]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:36:48 2008''
Retrieved from "https://proteopedia.org/1oaz"