SARS-CoV-2 virus proteins
From Proteopedia
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[[Image:SARS-Cov-2-genome.jpg|900px|left|thumb|SARS-CoV-2 Protein Organization, from Gordon | [[Image:SARS-Cov-2-genome.jpg|900px|left|thumb|SARS-CoV-2 Protein Organization, from Gordon | ||
| - | et al. & Krogan (2020)<ref> | + | et al. & Krogan (2020)<ref>[https://www.biorxiv.org/node/1214049.abstract]</ref>)]] |
* [[SARS-CoV-2 Coronavirus Main Protease| Main protease]]: it is a cysteine protease that is essential for the viral life cycle. | * [[SARS-CoV-2 Coronavirus Main Protease| Main protease]]: it is a cysteine protease that is essential for the viral life cycle. | ||
* [[SARS-CoV-2_protein_NSP1|NSP1]]: ''Host translation inhibitor nsp1''. Inhibits host translation by interacting with the 40S ribosomal subunit. | * [[SARS-CoV-2_protein_NSP1|NSP1]]: ''Host translation inhibitor nsp1''. Inhibits host translation by interacting with the 40S ribosomal subunit. | ||
Revision as of 07:55, 8 February 2022
| The quality of SARS-CoV-2 experimentally determined structures varies widely (Grabowski et al., 2021). Validated and corrected structures can be obtained from COVID19.BioReproducibility.Org. |
The genome of the SARS-CoV-2 virus codes for 28 proteins:
Out of those, 19 have already been characterized structurally. For the rest there are accurate AlphaFold2 predicted structures.
Details of the 3D structure & function of the key proteins & RNA inside the virus can be seen in the NY Times[2].
"The first viral protein created inside the infected cell, ORF1ab, is actually a chain of 16 proteins joined together. Two of these proteins act like scissors, snipping the links between the different proteins and freeing them to do their jobs."[2]
- Main protease: it is a cysteine protease that is essential for the viral life cycle.
- NSP1: Host translation inhibitor nsp1. Inhibits host translation by interacting with the 40S ribosomal subunit.
- NSP2: Non-structural protein 2.
- NSP3: Papain-like proteinase
- NSP4: Non-structural protein 4.
- NSP5: Proteinase 3CL-PRO
- AlphaFold2 Theoretical Model NSP6: Non-structural protein 6.
- NSP7: Non-structural protein 7.
- NSP8: Non-structural protein 8.
- NSP9: Non-structural protein 9.
- NSP10: Non-structural protein 10.
- RNA-directed RNA polymerase (RdRp)
- Helicase (Hel): Multi-functional protein with a zinc-binding domain in N-terminus
- Guanine-N7 methyltransferase (ExoN)
- Uridylate-specific endoribonuclease (NendoU)
- 2'-O-methyltransferase (2'-O-MT): Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs.
- Surface glycoprotein (S) and SARS-CoV-2 protein S priming by furin
- ORF3a: Forms homotetrameric potassium sensitive ion channels (viroporin) and may modulate virus release.
- Protein E: Plays a central role in virus morphogenesis and assembly.
- AlphaFold2 Theoretical Model Protein M: Component of the viral envelope.
- ORF6: Could be a determinant of virus virulence.
- ORF7a: Non-structural protein which is dispensable for virus replication in cell culture.
- ORF8: Open Reading Frame 8.
- AlphaFold2 Theoretical Model Protein N: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP).
- AlphaFold2 Theoretical Model ORF10: It is currently unclear whether this region translates into a functional protein.
References
- ↑ Holmes KV, Enjuanes L. Virology. The SARS coronavirus: a postgenomic era. Science. 2003 May 30;300(5624):1377-8. doi: 10.1126/science.1086418. PMID:12775826 doi:http://dx.doi.org/10.1126/science.1086418
- ↑ 2.0 2.1 NY Times (3-Apr-2020) Bad News Wrapped in Protein: Inside the Coronavirus Genome
- ↑ [1]
