Summary for 7QVK
| Entry DOI | 10.2210/pdb7qvk/pdb |
| Descriptor | Receptor tyrosine-protein kinase erbB-2, NM-02, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | receptor tyrosine protein kinase, oncoprotein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 84765.18 |
| Authors | |
| Primary citation | Sawmynaden, K.,Wong, N.,Davies, S.,Cowan, R.,Brown, R.,Tang, D.,Henry, M.,Tickle, D.,Matthews, D.,Carr, M.,Bakrania, P.,Hoi Ting, H.,Hall, G. Co-crystallisation and humanisation of an anti-HER2 single-domain antibody as a theranostic tool. Plos One, 18:e0288259-e0288259, 2023 Cited by PubMed Abstract: Human epidermal growth factor receptor-2 (HER2) is a well-recognised biomarker associated with 25% of breast cancers. In most cases, early detection and/or treatment correlates with an increased chance of survival. This study, has identified and characterised a highly specific anti-HER2 single-domain antibody (sdAb), NM-02, as a potential theranostic tool. Complete structural description by X-ray crystallography has revealed a non-overlapping epitope with current anti-HER2 antibodies. To reduce the immunogenicity risk, NM-02 underwent a humanisation process and retained wild type-like binding properties. To further de-risk the progression towards chemistry, manufacturing and control (CMC) we performed full developability profiling revealing favourable thermal and physical biochemical 'drug-like' properties. Finally, the application of the lead humanised NM-02 candidate (variant K) for HER2-specific imaging purposes was demonstrated using breast cancer HER2+/BT474 xenograft mice. PubMed: 37459326DOI: 10.1371/journal.pone.0288259 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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