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Official PDF TranslationActa Biochimica et Biophysica Sinica

Structural basis for the inhibition of coronaviral main proteases by PF-00835231

Authors: Xuelan Zhou; Xiaolu Lu; Cheng Lin; Xiaofang Zou; Wenwen Li; Xiangyi Zeng; Jie Wang; Pei Zeng; Weiwei Wang; Jin Zhang; Haihai Jiang; Jian Li

DOI: 10.3724/abbs.2024122Status: Verified Translated Edition
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Key Findings in This Report

• PF-00835231 exhibits broad-spectrum inhibition against various coronaviral main proteases, including SARS-CoV-2, SARS-CoV, and MERS-CoV, as well as seven clinically relevant mutants. • High-resolution crystal structures of Mpro-inhibitor complexes reveal key structural determinants and binding modes that explain the inhibitor's efficacy and adaptability. • The structural insights provide a rational basis for designing next-generation antivirals with improved oral bioavailability and broad-spectrum activity against emerging coronaviruses. • The study underscores the importance of targeting the highly conserved Mpro for developing therapeutic interventions against current and future coronavirus outbreaks.