Structure and conformational variability of the HER2-trastuzumab-pertuzumab complex

[Display omitted] •Antibodies Trastuzumab and Pertuzumab are effective in treating HER2-positive breast cancer.•A cryoEM structure of the HTP ternary complex allows detailed epitope-paratope views.•The structure suggests a further basis for the synergistic effect of trastuzumab and pertuzumab.•The d...

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Veröffentlicht in:	Journal of structural biology 2024-06, Vol.216 (2), p.108095-108095, Article 108095
Hauptverfasser:	Ruedas, Rémi, Vuillemot, Rémi, Tubiana, Thibault, Winter, Jean-Marie, Pieri, Laura, Arteni, Ana-Andreea, Samson, Camille, Jonic, Slavica, Mathieu, Magali, Bressanelli, Stéphane
Format:	Artikel
Sprache:	eng
Schlagworte:	Antibodies, Monoclonal, Humanized - chemistry Antibody-antigen complex Antigen-Antibody Complex - chemistry Biochemistry, Molecular Biology Cancer Continuous conformational variability Cryoelectron Microscopy - methods Cryogenic electron microscopy HER2 signaling Humans Life Sciences Models, Molecular Pharmaceutical sciences Pharmacology Protein Binding Protein Conformation Receptor, ErbB-2 - chemistry Receptor, ErbB-2 - metabolism Structural Biology Trastuzumab - chemistry
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