3CLp forms a homodimer

Stable Identifier
R-HSA-9694333
Type
Reaction [binding]
Species
Homo sapiens
Related Species
Severe acute respiratory syndrome coronavirus 2
Compartment
cytosol
ReviewStatus
5/5
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3CLp forms a homodimer
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The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
SARS-Cov-2 main protease forms a tight dimer. Dimerization of the enzyme is necessary for catalytic activity (Zhang et al, 2020; Davis et al, 2021).
Literature References
PubMed ID Title Journal Year
32198291 Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved α-ketoamide inhibitors

Hilgenfeld, R, Drosten, C, Curth, U, Sun, X, Rox, K, Zhang, L, Becker, S, Sauerhering, L, Lin, D

Science 2020
34399606 Regulation of the Dimerization and Activity of SARS-CoV-2 Main Protease through Reversible Glutathionylation of Cysteine 300

Mieyal, JJ, Wingfield, PT, Bulut, H, Jaeger, HK, Hattori, SI, Shrestha, P, Yaparla, A, Mitsuya, H, Davis, DA, Yarchoan, R

mBio 2021
Participants
Input
Output
Participates
as an event of
Disease
Name Identifier Synonyms
COVID-19 DOID:0080600 2019 Novel Coronavirus (2019-nCoV), Wuhan seafood market pneumonia virus infection, 2019-nCoV infection, Wuhan coronavirus infection
Authored
Stephan, R  (2020-07-30)
Reviewed
Acencio, ML  (2020-09-09)
Created
Cook, J  (2020-07-07)
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