13HA
The structure of Fab_C1 in complex with CD30
Summary for 13HA
| Entry DOI | 10.2210/pdb13ha/pdb |
| Descriptor | FabS1CE2_C1 heavy chain, FabS1CE2_C1 light chain (Trastuzumab Fab Light Chain), Tumor necrosis factor receptor superfamily member 8, ... (8 entities in total) |
| Functional Keywords | high-affinity binding, immune suppression, tumour growth suppressor, cell signalling, cytokine receptor, immune system |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 3 |
| Total formula weight | 59809.68 |
| Authors | Mallette, E.,Singer, A.U.,Blazer, L.L.,Adams, J.J.,Suits, M.D.L.,Sidhu, S.S. (deposition date: 2026-05-05, release date: 2026-09-30) |
| Primary citation | Mallette, E.,Blazer, L.L.,Hokanson, C.A.,Chen, C.,Perez, J.G.,Pavlenco, A.,Ploder, L.,Singer, A.U.,Suits, M.D.L.,Bhakta, S.,Junutula, J.R.,Adams, J.J.,Sidhu, S.S. Strategy for modular assembly of tetravalent, multispecific antibodies. Protein Sci., 35:e70797-e70797, 2026 Cited by PubMed Abstract: Multispecific, multivalent antibodies (Abs) are a burgeoning class of drugs that dramatically expand the pharmacological repertoire beyond traditional therapeutic Abs. Here, we present a simple, modular approach to developing multispecific, multivalent Abs based on a Fab-phage library with a single light chain. Using this library, we created three Abs targeting unique sites on programmed death-ligand 1 (PD-L1) and another antibody targeting CD30. Biophysical and cellular characterization of these Abs demonstrated their functional equivalence to clinically relevant Abs targeting PD-L1 or CD30. We then combined these paratopes into a series of bispecific, tetravalent, triparatopic Abs that retained the functionality of the parental Abs. Structural analysis of each of the Abs in complex with their cognate antigens demonstrated the adaptability of the common light chain to form diverse paratopes with an array of distinct heavy chains. PubMed: 42757708DOI: 10.1002/pro.70797 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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