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Updated: Apr 28, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
Expression, purification, crystallization and preliminary X-ray analysis of the HER3-9E12 Fab complex
Kecheng He1, Ang Huang2, Yong Huang3
1Key Laboratory of Oncology, Cancer Center, Chinese PLA General Hospital and Chinese PLA Medical School, Beijing 100853, People's Republic of China.
Abstract:
9E12 is a fully human immunoglobulin G1/κ monoclonal antibody that is specific for the epidermal growth factor receptor 3 (HER3), the overexpression of which has been detected in many tumour types and is associated with poor survival outcomes. To date, knowledge of the molecular mechanism for targeted antibodies that directly inhibit HER3 signalling is limited. Because knowledge of such therapeutic antibodies would help basic immunological therapeutics, structural insights into the HER3-9E12 Fab complex are important. Recombinant human HER3 and Fab fragments of the 9E12 antibody were cloned, expressed and crystallized, and crystallographic data sets were collected. The crystals belonged to space group P1, with unit-cell parameters a=74.4, b=98.6, c=99.6 Å, α=106.0, β=95.0, γ=102.5° and diffracted to a resolution of 2.1 Å.
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