nsp9 forms a homotetramer

Stable Identifier
R-HSA-9694261
Type
Reaction [uncertain]
Species
Homo sapiens
Related Species
Severe acute respiratory syndrome coronavirus 2
Compartment
cytosol
ReviewStatus
5/5
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nsp9 forms a homotetramer
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Nonstructural protein 9 from SARS-Cov-2 is an obligate homodimer, comprising a unique fold that associates via an unusual α-helical GxxxG interaction motif. The integrity of this motif is considered important for viral replication (Littler et al, 2020; Miknis et al, 2009). The dimer units associate to form tetramers (Zhang et al, 2020).
Literature References
PubMed ID Title Journal Year
34765992 Structural basis for the multimerization of nonstructural protein nsp9 from SARS-CoV-2

Zhang, C, Chen, Y, Li, L, Yang, Y, He, J, Chen, C, Su, D

Mol Biomed 2020
32592996 Crystal Structure of the SARS-CoV-2 Non-structural Protein 9, Nsp9

Littler, DR, Gully, BS, Colson, RN, Rossjohn, J

iScience 2020
19153232 Severe acute respiratory syndrome coronavirus nsp9 dimerization is essential for efficient viral growth

Miknis, ZJ, Donaldson, EF, Umland, TC, Rimmer, RA, Baric, RS, Schultz, LW

J. Virol. 2009
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
Cross References
Mondo
Authored
Stephan, R  (2020-07-30)
Reviewed
Acencio, ML  (2020-09-09)
Created
Cook, J  (2020-07-07)
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