9P1M
Cryo-EM structure of CD73 in complex with antibody Sym024
Summary for 9P1M
| Entry DOI | 10.2210/pdb9p1m/pdb |
| EMDB information | 71128 |
| Descriptor | 5'-nucleotidase, Antibody Light Chain, Antibody Heavy Chain, ... (5 entities in total) |
| Functional Keywords | antigen-antibody complex, drug target, hydrolase |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 6 |
| Total formula weight | 265342.34 |
| Authors | Bansia, H.,Armbruster, E.,Des Georges, A. (deposition date: 2025-06-10, release date: 2025-12-24, Last modification date: 2026-01-21) |
| Primary citation | Jakobsen, J.S.,Grandal, M.M.,Hansen, R.W.,Bansia, H.,Armbruster, E.,Theret, I.,Skartved, N.J.O.,Hald, R.,Melander, M.C.,Worsaae, A.,Riva, M.,Reckzeh, K.,Vuillard, L.,Lantto, J.,des Georges, A.,Frohlich, C. Sym024 interacts with a unique epitope on the CD73 homodimer, favoring effective bivalent binding to improve anti-PD1 therapy. Clin.Cancer Res., 2026 Cited by PubMed Abstract: Adenosine signaling may be a central immune suppressive mechanism in several cancers, and blockade of the rate-limiting CD73 AMP-to-adenosine enzyme has been demonstrated to improve clinical efficacy of PD(L)-1 immune therapy. However, deep inhibition of CD73 activity could prove difficult in tumor environments with a constant AMP supply and high CD73 levels. Here, we sought to identify, characterize, and benchmark a novel antagonistic anti-CD73 antibody, Sym024 (S95024), and to structurally decode its mode of action. PubMed: 41511395DOI: 10.1158/1078-0432.CCR-25-2406 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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