9IUT

Crystal structure of cancer-specific anti-HER2 antibody H2Mab-250 in complex with epitope peptide

Summary for 9IUT

• Entry DOI: 10.2210/pdb9iut/pdb
• Descriptor: H2Mab-250 VH(S112C)-SARAH, H2Mab-250 VL-SARAH(S37C), H2Mab-250 epitope peptide, ... (4 entities in total)
• Functional Keywords: fv-clasp, antibody, cancer-specific, her2, immune system
• Biological source: Mus musculus; More
• Total number of polymer chains: 6
• Total formula weight: 77962.30

Authors

Arimori, T.,Takagi, J. (deposition date: 2024-07-22, release date: 2025-06-04)

• Primary citation: Hosking, M.P.,Shirinbak, S.,Omilusik, K.,Chandra, S.,Kaneko, M.K.,Gentile, A.,Yamamoto, S.,Shrestha, B.,Grant, J.,Boyett, M.,Cardenas, D.,Keegan, H.,Ibitokou, S.,Pavon, C.,Mizoguchi, T.,Ihara, T.,Nakayama, D.,Abujarour, R.,Lee, T.T.,Clarke, R.,Goodridge, J.,Peralta, E.,Maeda, T.,Takagi, J.,Arimori, T.,Kato, Y.,Valamehr, B.; Preferential tumor targeting of HER2 by iPSC-derived CAR-T cells engineered to overcome multiple barriers to solid tumor efficacy.; Cell Stem Cell, 2025; DOI: 10.1016/j.stem.2025.05.007

Experimental method

X-RAY DIFFRACTION (2.09 Å)