1yy8

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[[Image:1yy8.png|left|200px]]
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==Crystal structure of the Fab fragment from the monoclonal antibody cetuximab/Erbitux/IMC-C225==
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<StructureSection load='1yy8' size='340' side='right' caption='[[1yy8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1yy8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YY8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YY8 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yy9|1yy9]]</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yy8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yy8 RCSB], [http://www.ebi.ac.uk/pdbsum/1yy8 PDBsum]</span></td></tr>
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<table>
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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/yy/1yy8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata 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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Recent structural studies of epidermal growth factor receptor (EGFR) family extracellular regions have identified an unexpected mechanism for ligand-induced receptor dimerization that has important implications for activation and inhibition of these receptors. Here we describe the 2.8 angstroms resolution X-ray crystal structure of the antigen binding (Fab) fragment from cetuximab (Erbitux), an inhibitory anti-EGFR antibody, in complex with the soluble extracellular region of EGFR (sEGFR). The sEGFR is in the characteristic "autoinhibited" or "tethered" inactive configuration. Cetuximab interacts exclusively with domain III of sEGFR, partially occluding the ligand binding region on this domain and sterically preventing the receptor from adopting the extended conformation required for dimerization. We suggest that both these effects contribute to potent inhibition of EGFR activation.
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{{STRUCTURE_1yy8| PDB=1yy8 | SCENE= }}
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Structural basis for inhibition of the epidermal growth factor receptor by cetuximab.,Li S, Schmitz KR, Jeffrey PD, Wiltzius JJ, Kussie P, Ferguson KM Cancer Cell. 2005 Apr;7(4):301-11. PMID:15837620<ref>PMID:15837620</ref>
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===Crystal structure of the Fab fragment from the monoclonal antibody cetuximab/Erbitux/IMC-C225===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_15837620}}
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==About this Structure==
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[[1yy8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YY8 OCA].
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==See Also==
==See Also==
*[[Monoclonal Antibody|Monoclonal Antibody]]
*[[Monoclonal Antibody|Monoclonal Antibody]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:015837620</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Ferguson, K M.]]
[[Category: Ferguson, K M.]]

Revision as of 23:19, 28 September 2014

Crystal structure of the Fab fragment from the monoclonal antibody cetuximab/Erbitux/IMC-C225

1yy8, resolution 2.00Å

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