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Article

Conformational Flexibility of a Short Loop near the Active Site of the SARS-3CLpro is Essential to Maintain Catalytic Activity.

Scientific reports - 16 Feb 2016

Li Chunmei, Teng Xin, Qi Yifei, Tang Bo, Shi Hailing, Ma Xiaomin, Lai Luhua

Abstract excerpt

The SARS 3C-like proteinase (SARS-3CLpro), which is the main proteinase of the SARS coronavirus, is essential to the virus life cycle. This enzyme has been shown to be active as a dimer in which only one protomer is active. However, it remains unknown how the dimer structure maintains an active monomer conformation. It has been observed that the Ser139-Leu141 loop forms a short 3(10)-helix that disrupts the...

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Identifiers

PMID: 26879383
DOI: 10.1038/srep20918
PMCID: PMC4754693

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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