9KFW
NMR structure of an agonistic OX40 nanobody
Summary for 9KFW
| Entry DOI | 10.2210/pdb9kfw/pdb |
| Descriptor | nanobody (1 entity in total) |
| Functional Keywords | antibody, nanobody, protein binding |
| Biological source | Vicugna pacos |
| Total number of polymer chains | 1 |
| Total formula weight | 13947.24 |
| Authors | Nagata, T.,Kobayashi, N.,Iemura, T.,Kitawaki, T.,Maeda, R.,Nagata, K.,Yamazaki, K.,Shirakawa, K.,Imura, A.,Takaori-Kondo, A. (deposition date: 2024-11-07, release date: 2025-11-12, Last modification date: 2026-08-26) |
| Primary citation | Iemura, T.,Kitawaki, T.,Maeda, R.,Mitsuyoshi, T.,Nagata, K.,Yamazaki, H.,Shirakawa, K.,Kobayashi, N.,Nagata, T.,Imura, A.,Takaori-Kondo, A. Efficient discovery of an agonistic anti-OX40 nanobody by epitope-directed approach to address enrichment-driven epitope bias. J Immunother Cancer, 14:-, 2026 Cited by PubMed Abstract: Conventional antibody discovery approaches that do not account for enrichment-driven biases, such as epitope immunogenicity, PCR amplification bias, or protein expression efficiency, may result in under-representation of rare yet functionally relevant clones, necessitating labor-intensive in vitro screening to identify agonistic antibodies among a large number of dominant clones. Thus, efficient screening methods for agonistic antibodies are urgently needed. OX40 is a promising target for cancer immunotherapy due to its role in enhancing T-cell activation and survival. However, effective anti-OX40 agonistic antibodies have not yet been developed. PubMed: 42547263DOI: 10.1136/jitc-2025-014419 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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