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Article

Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure.

Virology - 5 Jun 2009

Hu Tiancen, Zhang Yu, Li Lianwei, Wang Kuifeng, Chen Shuai, Chen Jing, Ding Jianping, Jiang Hualiang, Shen Xu

Abstract excerpt

The 3C-like protease of SARS coronavirus (SARS-CoV 3CL(pro)) is vital for SARS-CoV replication and is a promising drug target. It has been extensively proved that only the dimeric enzyme is active. Here we discovered that two adjacent mutations (Ser139_Ala and Phe140_Ala) on the dimer interface resulted in completely different crystal structures of the enzyme, demonstrating the distinct roles of these two...

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Source

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Identifiers

PMID: 19409595
DOI: 10.1016/j.virol.2009.03.034
PMCID: PMC7103376

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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