6axp
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of cetuximab with aminoheptanoic acid-linked n-octylarginine meditope variant== | |
| + | <StructureSection load='6axp' size='340' side='right' caption='[[6axp]], [[Resolution|resolution]] 2.48Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6axp]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AXP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AXP FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=011:7-AMINOHEPTANOIC+ACID'>011</scene>, <scene name='pdbligand=C1J:'>C1J</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ido|5ido]], [[6au5|6au5]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6axp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6axp OCA], [http://pdbe.org/6axp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6axp RCSB], [http://www.ebi.ac.uk/pdbsum/6axp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6axp ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Meditope, a cyclic 12-residue peptide, binds to a unique binding side between the light and heavy chains of the cetuximab Fab. In an effort to improve the affinity of the interaction, it was sought to extend the side chain of Arg8 in the meditope, a residue that is accessible from the other side of the meditope binding site, in order to increase the number of interactions. These modifications included an n-butyl and n-octyl extension as well as hydroxyl, amine and carboxyl substitutions. The atomic structures of the complexes and the binding kinetics for each modified meditope indicated that each extension threaded through the Fab `hole' and that the carboxyethylarginine substitution makes a favorable interaction with the Fab, increasing the half-life of the complex by threefold compared with the unmodified meditope. Taken together, these studies provide a basis for the design of additional modifications to enhance the overall affinity of this unique interaction. | ||
| - | + | Meditope-Fab interaction: threading the hole.,Bzymek KP, Ma Y, Avery KN, Horne DA, Williams JC Acta Crystallogr F Struct Biol Commun. 2017 Dec 1;73(Pt 12):688-694. doi:, 10.1107/S2053230X17016272. Epub 2017 Nov 18. PMID:29199990<ref>PMID:29199990</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: Bzymek, K | + | <div class="pdbe-citations 6axp" style="background-color:#fffaf0;"></div> |
| - | [[Category: Williams, J | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bzymek, K P]] | ||
| + | [[Category: Williams, J C]] | ||
| + | [[Category: Anti-egfr]] | ||
| + | [[Category: Antibody]] | ||
| + | [[Category: Immune system]] | ||
Revision as of 07:01, 13 December 2017
Structure of cetuximab with aminoheptanoic acid-linked n-octylarginine meditope variant
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