Statistical crystallography reveals an allosteric network in SARS-CoV-2 Mpro
Anne Creon, T. Emilie S. Scheer, Patrick Reinke, Aida Rahmani Mashhour, Sebastian Günther, Stephan Niebling, Kira Schamoni-Kast, Charlotte Uetrecht, Alke Meents, Henry N. Chapman, Janina Sprenger, Thomas J. Lane · 2026
Read Statistical crystallography reveals an allosteric network in SARS-CoV-2 Mpro by Anne Creon, T. Emilie S. Scheer, Patrick Reinke, Aida Rahmani Mashhour, Sebastian Günther, Stephan Niebling, Kira Schamoni-Kast, Charlotte Uetrecht, Alke Meents, Henry N. Chapman, Janina Sprenger, Thomas J. Lane (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-13135515.txt.
Description
Anne Creon and a team of co-authors mine more than a thousand crystal snapshots of the main protease of the COVID virus. Their study is from two thousand twenty-six. The protease is a key drug target. It switches on only when two copies join together, and signals inside the protein must travel from the join site to the cutting site.
From the pile of structures, the team modeled how the protein flexes in its natural state. The model predicted which spots in the joining region move in step with the cutting site. Mutating those spots cut activity sharply in one case, mildly in another, and not at all in a third. Follow-up tests explained why each case differed. The method can reveal hidden control networks in other proteins too.
Catalog record
| CREATOR | Anne Creon, T. Emilie S. Scheer, Patrick Reinke, Aida Rahmani Mashhour, Sebastian Günther, Stephan Niebling, Kira Schamoni-Kast, Charlotte Uetrecht, Alke Meents, Henry N. Chapman, Janina Sprenger, Thomas J. Lane |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 107 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |