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Article

Structural basis for inhibition of the epidermal growth factor receptor by cetuximab.

Cancer cell - 1 Apr 2005

Li Shiqing, Schmitz Karl R, Jeffrey Philip D, Wiltzius Jed J W, Kussie Paul, Ferguson Kathryn M

Abstract excerpt

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...

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Topics

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Share to Antibodies, Monoclonal, Humanized
Share to Antigen-Antibody Complex

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Binding, Competitive

Share to Cetuximab

Share to Epidermal Growth Factor

Share to Immunoglobulin Fab Fragments

Share to Protein Structure, Quaternary

Share to Transforming Growth Factor alpha

Source

Identifiers

PMID: 15837620
DOI: 10.1016/j.ccr.2005.03.003

Genes

EGFR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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