2bx5: Difference between revisions
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New page: left|200px<br /> <applet load="2bx5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bx5, resolution 2.7Å" /> '''IS FR1 THE ANTIBODY'... |
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== | ==Is FR1 the antibody's Achillies heel== | ||
Antibodies are the archetypal molecules of the Ig-fold superfamily. Their | <StructureSection load='2bx5' size='340' side='right'caption='[[2bx5]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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=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> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9UL77_HUMAN Q9UL77_HUMAN] | |||
== 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/bx/2bx5_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=2bx5 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2bx5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: James LC]] | ||
Latest revision as of 07:47, 23 October 2024
Is FR1 the antibody's Achillies heel
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