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New page: left|200px<br /> <applet load="2a6d" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a6d, resolution 2.9Å" /> '''Crystal structure an...
 
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[[Image:2a6d.gif|left|200px]]<br />
<applet load="2a6d" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2a6d, resolution 2.9&Aring;" />
'''Crystal structure analysis of the anti-arsonate germline antibody 36-65 in complex with a phage display derived dodecapeptide RLLIADPPSPRE'''<br />


==Overview==
==Crystal structure analysis of the anti-arsonate germline antibody 36-65 in complex with a phage display derived dodecapeptide RLLIADPPSPRE==
The limited primary antibody repertoire uses multiple mechanisms to, account for the large number of potential antigens. In this issue of, Immunity, Sethi et al. (2006) describe a new means for expanding the, antibody repertoire, whereby a single antibody isomer binds diverse, antigens at different regions of the binding site.
<StructureSection load='2a6d' size='340' side='right'caption='[[2a6d]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2a6d]] is a 5 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=2A6D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A6D 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]] 2.9&#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=2a6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a6d OCA], [https://pdbe.org/2a6d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a6d RCSB], [https://www.ebi.ac.uk/pdbsum/2a6d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a6d ProSAT]</span></td></tr>
</table>
== 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/a6/2a6d_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2a6d ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Correlation between the promiscuity of the primary antibody response and conformational flexibility in a germline antibody was addressed by using germline antibody 36-65. Crystallographic analyses of the 36-65 Fab with three independent dodecapeptides provided mechanistic insights into the generation of antibody diversity. While four antigen-free Fab molecules provided a quantitative description of the conformational repertoire of the antibody CDRs, three Fab molecules bound to structurally diverse peptide epitopes exhibited a common paratope conformation. Each peptide revealed spatially different footprints within the antigen-combining site. However, a conformation-specific lock involving two shared residues, which were also associated with hapten binding, was discernible. Unlike the hapten, the peptides interacted with residues that undergo somatic mutations, suggesting a possible mechanism for excluding "nonspecific" antigens during affinity maturation. The observed multiple binding modes of diverse epitopes within a common paratope conformation of a germline antibody reveal a simple, yet elegant, mechanism for expanding the primary antibody repertoire.


==About this Structure==
Differential epitope positioning within the germline antibody paratope enhances promiscuity in the primary immune response.,Sethi DK, Agarwal A, Manivel V, Rao KV, Salunke DM Immunity. 2006 Apr;24(4):429-38. PMID:16618601<ref>PMID:16618601</ref>
2A6D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A6D OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Multiple paths to multispecificity., Mariuzza RA, Immunity. 2006 Apr;24(4):359-61. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16618592 16618592]
</div>
<div class="pdbe-citations 2a6d" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Antibody 3D structures|Antibody 3D structures]]
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Agarwal A]]
[[Category: Agarwal, A.]]
[[Category: Manivel V]]
[[Category: Manivel, V.]]
[[Category: Rao KV]]
[[Category: Rao, K.V.]]
[[Category: Salunke DM]]
[[Category: Salunke, D.M.]]
[[Category: Sethi DK]]
[[Category: Sethi, D.K.]]
[[Category: antibody]]
[[Category: fab]]
[[Category: germline]]
 
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