1yy8: Difference between revisions
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== 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/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> | ||
</td></tr><tr><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><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://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 == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Ferguson, K M | [[Category: Ferguson, K M]] | ||
[[Category: Jeffrey, P D | [[Category: Jeffrey, P D]] | ||
[[Category: Kussie, P | [[Category: Kussie, P]] | ||
[[Category: Li, S | [[Category: Li, S]] | ||
[[Category: Schmitz, K R | [[Category: Schmitz, K R]] | ||
[[Category: Wiltzius, J J.W | [[Category: Wiltzius, J J.W]] | ||
[[Category: Antibody drug]] | [[Category: Antibody drug]] | ||
[[Category: Cancer]] | [[Category: Cancer]] | ||
[[Category: Fab fragment]] | [[Category: Fab fragment]] | ||
[[Category: Immune system]] | [[Category: Immune system]] | ||
Revision as of 12:11, 8 January 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
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 PubMedRecent 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 AlsoReferences
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