1yy8: Difference between revisions

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<StructureSection load='1yy8' size='340' side='right' caption='[[1yy8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1yy8' size='340' side='right' caption='[[1yy8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[1yy8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yy9|1yy9]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yy9|1yy9]]</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=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>
<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=1yy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yy8 OCA], [http://pdbe.org/1yy8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yy8 RCSB], [http://www.ebi.ac.uk/pdbsum/1yy8 PDBsum]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 1yy8" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Lk3 transgenic mice]]
[[Category: Ferguson, K M]]
[[Category: Ferguson, K M]]
[[Category: Jeffrey, P D]]
[[Category: Jeffrey, P D]]

Revision as of 12:10, 11 September 2015

Crystal structure of the Fab fragment from the monoclonal antibody cetuximab/Erbitux/IMC-C225Crystal structure of the Fab fragment from the monoclonal antibody cetuximab/Erbitux/IMC-C225

Structural highlights

1yy8 is a 4 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Li S, Schmitz KR, Jeffrey PD, Wiltzius JJ, Kussie P, Ferguson KM. Structural basis for inhibition of the epidermal growth factor receptor by cetuximab. Cancer Cell. 2005 Apr;7(4):301-11. PMID:15837620 doi:10.1016/j.ccr.2005.03.003

1yy8, resolution 2.00Å

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