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Cooperativity and communication between the active sites of the dimeric SARS-CoV-2 main protease.

Science advances - 16 Jan 2026

Zvornicanin Sarah N, Shaqra Ala M, Flynn Julia, Intravaia Lauren E, Martinez Heidi Carias, Jia Weiping, Gupta Devendra Kumar, Moquin Stephanie, Dovala Dustin, Bolon Daniel N, Kelch Brian A, Schiffer Celia A, Yilmaz Nese Kurt

Abstract excerpt

The coronaviral main protease (Mpro) has been the subject of various biochemical and structural studies and a drug target against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infections. SARS-CoV-2 Mpro is active as a dimer, but despite apparent cooperativity in catalytic activity, how the two distal active sites communicate and modulate binding and/or catalysis is unclear. Here, we have...

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Catalytic Domain
Coronavirus 3C Proteases
Crystallography, X-Ray
Models, Molecular
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Binding

Protein Multimerization

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Identifiers

PMID: 41544157
DOI: 10.1126/sciadv.aeb0769
PMCID: PMC12810614

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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