The structure of the anti-c-myc antibody 9E10 Fab fragment/epitope peptide complex reveals a novel binding mode dominated by the heavy chain hypervariable loops |
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| Authors: | Krauss Norbert Wessner Helga Welfle Karin Welfle Heinz Scholz Christa Seifert Martina Zubow Kristina Aÿ Jacqueline Hahn Michael Scheerer Patrick Skerra Arne Höhne Wolfgang |
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| Institution: | 1. Institut für Biochemie, Charité, Universit?tsmedizin Berlin, Monbijoustr. 2, D‐10117 Berlin, Germany;2. Current address: School of Biological and Chemical Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS, UK;3. Max‐Delbrück‐Centrum für Molekulare Medizin, Robert‐R?ssle‐Str. 10, D‐13122 Berlin‐Buch, Germany;4. Institut für Medizinische Immunologie, Charité‐Universit?tsmedizin Berlin, Schumannstr 20/21, D‐10117 Berlin, Germany;5. Lehrstuhl für Biologische Chemie, Technische Universit?t München, An der Saatzucht 5, D‐85350 Freising‐Weihenstephan, Germany |
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| Abstract: | The X-ray structure of the Fab fragment from the anti-c-myc antibody 9E10 was determined both as complex with its epitope peptide and for the free Fab. In the complex, two Fab molecules adopt an unusual head to head orientation with the epitope peptide arranged between them. In contrast, the free Fab forms a dimer with different orientation. In the Fab/peptide complex the peptide is bound to one of the two Fabs at the "back" of its extended CDR H3, in a cleft with CDR H1, thus forming a short, three-stranded antiparallel beta-sheet. The N- and C-terminal parts of the peptide are also in contact with the neighboring Fab fragment. Comparison between the CDR H3s of the two Fab molecules in complex with the peptide and those from the free Fab reveals high flexibility of this loop. This structural feature is in line with thermodynamic data from isothermic titration calorimetry. |
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| Keywords: | antibody‐antigen interaction epitope peptide myc‐tag crystal structure conformation of complementarity determining regions calorimetry |
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