8V52
Crystal structure of 2A10 Fab bound to Human TGF-beta3
Summary for 8V52
| Entry DOI | 10.2210/pdb8v52/pdb |
| Descriptor | Transforming growth factor beta-3, 2A10 Fab Light chain, 2A10 Fab Heavy Chain, ... (4 entities in total) |
| Functional Keywords | tgf beta, 2a10, complex, fab, cytokine, cytokine-immune system complex, cytokine/immune system |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 6 |
| Total formula weight | 121433.79 |
| Authors | Yin, J.,Lupardus, P.J. (deposition date: 2023-11-30, release date: 2024-04-10, Last modification date: 2024-11-13) |
| Primary citation | Sun, T.,Vander Heiden, J.A.,Gao, X.,Yin, J.,Uttarwar, S.,Liang, W.C.,Jia, G.,Yadav, R.,Huang, Z.,Mitra, M.,Halpern, W.,Bender, H.S.,Brightbill, H.D.,Wu, Y.,Lupardus, P.,Ramalingam, T.,Arron, J.R. Isoform-selective TGF-beta 3 inhibition for systemic sclerosis. Med, 5:132-147.e7, 2024 Cited by PubMed Abstract: Transforming growth factor β (TGF-β) is implicated as a key mediator of pathological fibrosis, but its pleiotropic activity in a range of homeostatic functions presents challenges to its safe and effective therapeutic targeting. There are three isoforms of TGF-β, TGF-β1, TGF-β2, and TGF-β3, which bind to a common receptor complex composed of TGF-βR1 and TGF-βR2 to induce similar intracellular signals in vitro. We have recently shown that the cellular expression patterns and activation thresholds of TGF-β2 and TGF-β3 are distinct from those of TGF-β1 and that selective short-term TGF-β2 and TGF-β3 inhibition can attenuate fibrosis in vivo without promoting excessive inflammation. Isoform-selective inhibition of TGF-β may therefore provide a therapeutic opportunity for patients with chronic fibrotic disorders. PubMed: 38272035DOI: 10.1016/j.medj.2023.12.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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