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Structure of the Fab fragment of the anti-murine EGFR antibody 7A7 and exploration of its receptor binding site.

Journal article
Authors Ariel Talavera
Jenny Mackenzie
Greta Garrido
Rosmarie Friemann
Alejandro López-Requena
Ernesto Moreno
Ute Krengel
Published in Molecular immunology
Volume 48
Issue 12-13
Pages 1578-85
ISSN 1872-9142
Publication year 2011
Published at Department of Chemistry
Pages 1578-85
Language en
Keywords Amino Acid Sequence, Animals, Antibodies, Monoclonal, chemistry, immunology, metabolism, Antigen-Antibody Complex, Binding Sites, Antibody, Cross Reactions, Crystallography, X-Ray, Immunoglobulin Fab Fragments, chemistry, metabolism, Mice, Models, Molecular, Protein Conformation, Protein-Tyrosine Kinases, antagonists & inhibitors, Receptor, Epidermal Growth Factor, immunology, metabolism, Static Electricity
Subject categories Structural Biology


The EGF receptor is an important target of cancer immunotherapies. The 7A7 monoclonal antibody has been raised against the murine EGFR, but it cross-reacts with the human receptor. The results from experiments using immune-competent mice can therefore, in principle, be extrapolated to the corresponding scenario in humans. In this work we report the crystal structure of the 7A7 Fab at an effective resolution of 1.4Å. The antibody binding site comprises a deep pocket, located at the interface between the light and heavy chains, with major contributions from CDR loops H1, H2, H3 and L1. Binding experiments show that 7A7 recognizes a site on the EGFR extracellular domain that is not accessible in its most stable conformations, but that becomes exposed upon treatment with a tyrosine kinase inhibitor. This suggests a recognition mechanism similar to that proposed for mAb 806.

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