7OM4
Nanobody EgB4 bound to the full extracellular EGFR-EGF complex
Summary for 7OM4
Entry DOI | 10.2210/pdb7om4/pdb |
Descriptor | Epidermal growth factor receptor, Epidermal growth factor, Nanobody EgB4, ... (4 entities in total) |
Functional Keywords | egfr, nanobody, cancer, signaling, immune system |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 3 |
Total formula weight | 91682.24 |
Authors | Zeronian, M.R.,Janssen, B.J.C. (deposition date: 2021-05-21, release date: 2022-03-02, Last modification date: 2024-11-13) |
Primary citation | Zeronian, M.R.,Doulkeridou, S.,van Bergen En Henegouwen, P.M.P.,Janssen, B.J.C. Structural insights into the non-inhibitory mechanism of the anti-EGFR EgB4 nanobody. Bmc Mol Cell Biol, 23:12-12, 2022 Cited by PubMed Abstract: The epidermal growth factor receptor (EGFR) is involved in various developmental processes, and alterations of its extracellular segment are associated with several types of cancers, in particular glioblastoma multiforme (GBM). The EGFR extracellular region is therefore a primary target for therapeutic agents, such as monoclonal antibodies and variable domains of heavy chain antibodies (VHH), also called nanobodies. Nanobodies have been previously shown to bind to EGFR, and to inhibit ligand-mediated EGFR activation. PubMed: 35232398DOI: 10.1186/s12860-022-00412-x PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (6.05 Å) |
Structure validation
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