Ontology highlight
ABSTRACT:
SUBMITTER: Ravanfar R
PROVIDER: S-EPMC9161685 | biostudies-literature | 2022 Sep
REPOSITORIES: biostudies-literature
Ravanfar Raheleh R Sheng Yuling Y Shahgholi Mona M Lomenick Brett B Jones Jeff J Chou Tsui-Fen TF Gray Harry B HB Winkler Jay R JR
Journal of inorganic biochemistry 20220602
The SARS-CoV-2 main protease (M<sup>pro</sup>) is responsible for cleaving twelve nonstructural proteins from the viral polyprotein. M<sup>pro</sup>, a cysteine protease, is characterized by a large number of noncatalytic cysteine (Cys) residues, none involved in disulfide bonds. In the absence of a tertiary-structure stabilizing role for these residues, a possible alternative is that they are involved in redox processes. We report experimental work in support of a proposal that surface cysteine ...[more]