1yy8: Difference between revisions

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

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

~~==Overview==~~

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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.

The line below this paragraph, {{ABSTRACT_PUBMED_15837620}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15837620 is the PubMed ID number.

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==About this Structure==

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[[Category: Cancer]]

[[Category: Fab fragment]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 16~~:57:04 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:27:58 2008''

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-[[Image:1yy8.gif|left|200px]]
+{{Seed}}
+[[Image:1yy8.png|left|200px]]
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 {{STRUCTURE_1yy8|  PDB=1yy8  |  SCENE=  }}
-'''Crystal structure of the Fab fragment from the monoclonal antibody cetuximab/Erbitux/IMC-C225'''
+===Crystal structure of the Fab fragment from the monoclonal antibody cetuximab/Erbitux/IMC-C225===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15837620}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15837620 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15837620}}
 ==About this Structure==
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 [[Category: Cancer]]
 [[Category: Fab fragment]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:57:04 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:27:58 2008''