Structural analysis of the flexibility of the Ubl2 domain within the papain-like protease of SARS-CoV-2
Gian Luca Freiherr von Scholley, Martina Schaefer, Mark D. Tully, Marc-Andre Hograindleur, Montserrat Soler-López, Roman C. Hillig, Christoph Mueller-Dieckmann, Eaazhisai Kandiah · 2026
Read Structural analysis of the flexibility of the Ubl2 domain within the papain-like protease of SARS-CoV-2 by Gian Luca Freiherr von Scholley, Martina Schaefer, Mark D. Tully, Marc-Andre Hograindleur, Montserrat Soler-López, Roman C. Hillig, Christoph Mueller-Dieckmann, Eaazhisai Kandiah (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13224804.txt.
Description
Freiherr von Scholley and co-authors catch a viral enzyme in the act of flexing, in this 2026 study. The enzyme is the papain-like protease of SARS-CoV-2, which the virus needs to copy itself and to dodge the immune system. One of its two domains, a ubiquitin-like piece, was thought to swivel freely, yet nearly every stored structure shows it locked shut.
Their new crystal structure holds the domain in both poses at once: the familiar closed one and a new open one, shifted by four angstroms. A zinc ion's presence in a nearby finger seems to tip the balance. The authors say the wobble is real and could be drugged. Flexibility, once doubted, is now on record.
Catalog record
| CREATOR | Gian Luca Freiherr von Scholley, Martina Schaefer, Mark D. Tully, Marc-Andre Hograindleur, Montserrat Soler-López, Roman C. Hillig, Christoph Mueller-Dieckmann, Eaazhisai Kandiah |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 29 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |