2bx5

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[[Image:2bx5.jpg|left|200px]]<br /><applet load="2bx5" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2bx5, resolution 2.7&Aring;" />
 
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'''IS FR1 THE ANTIBODY'S ACHILLIES HEEL'''<br />
 
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==Overview==
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==Is FR1 the antibody's Achillies heel==
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Antibodies are the archetypal molecules of the Ig-fold superfamily. Their, highly conserved beta-sheet architecture has evolved to avoid aggregation, by protecting edge strands. However, the crystal structure of a human V, kappa domain described here, reveals an exposed beta-edge strand which, mediates assembly of a helical pentadecameric oligomer. This edge strand, is highly conserved in V kappa domains but is both shortened and capped by, the use of two sequential trans-proline residues in V lambda domains. We, suggest that the exposure of this beta-edge in V kappa domains may explain, why light-chain deposition disease is mediated predominantly by kappa, antibodies.
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<StructureSection load='2bx5' size='340' side='right'caption='[[2bx5]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2bx5]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BX5 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]] 2.7&#8491;</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=2bx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bx5 OCA], [https://pdbe.org/2bx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bx5 RCSB], [https://www.ebi.ac.uk/pdbsum/2bx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bx5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9UL77_HUMAN Q9UL77_HUMAN]
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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/bx/2bx5_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=2bx5 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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Antibodies are the archetypal molecules of the Ig-fold superfamily. Their highly conserved beta-sheet architecture has evolved to avoid aggregation by protecting edge strands. However, the crystal structure of a human V kappa domain described here, reveals an exposed beta-edge strand which mediates assembly of a helical pentadecameric oligomer. This edge strand is highly conserved in V kappa domains but is both shortened and capped by the use of two sequential trans-proline residues in V lambda domains. We suggest that the exposure of this beta-edge in V kappa domains may explain why light-chain deposition disease is mediated predominantly by kappa antibodies.
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==About this Structure==
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Beta-edge interactions in a pentadecameric human antibody V kappa domain.,James LC, Jones PC, McCoy A, Tennent GA, Pepys MB, Famm K, Winter G J Mol Biol. 2007 Mar 30;367(3):603-8. Epub 2006 Nov 3. PMID:17292396<ref>PMID:17292396</ref>
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2BX5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BX5 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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Beta-edge interactions in a pentadecameric human antibody V kappa domain., James LC, Jones PC, McCoy A, Tennent GA, Pepys MB, Famm K, Winter G, J Mol Biol. 2007 Mar 30;367(3):603-8. Epub 2006 Nov 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17292396 17292396]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 2bx5" 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: aggregation]]
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__TOC__
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[[Category: amyloid]]
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</StructureSection>
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[[Category: antibody]]
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[[Category: Homo sapiens]]
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[[Category: fr1]]
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[[Category: Large Structures]]
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[[Category: lcdd]]
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[[Category: James LC]]
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[[Category: light-chain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:17:34 2008''
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Current revision

Is FR1 the antibody's Achillies heel

PDB ID 2bx5

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