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Updated: Jun 5, 2026

Production of Human Norovirus Protruding Domains in E. coli for X-ray Crystallography
Published on: April 19, 2016
Functional consequences of mutational analysis of norovirus protease
Yuichi Someya1, Naokazu Takeda
1Department of Virology II, National Institute of Infectious Diseases, Tokyo, Japan. someya@nih.go.jp
Abstract:
Norovirus protease has been subjected to an extensive mutagenesis study. Ala-scanning mutation at 13 different positions (Trp6, Trp19, Thr27, Leu86, Leu95, Leu97, Met101, Gln117, Leu121, Thr134, Tyr143, Val144, and Val167) led to loss of function and/or stability. Considering the crystal structure of the protease, it was revealed that a hydroxyl group of Thr134 and an aromatic ring of Tyr143 were important for substrate recognition along with His157. It was notable that several of the residues identified were in close proximity to each other, suggesting their importance for the integrity and stability of the protease.
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