Crystal structures of SARS-CoV-2 ADP-ribose phosphatase: from the apo form to ligand complexes.
ADP-ribose phosphatase domain
ADP-ribosylation
ADRP
COVID-19
Mac1
Nsp3
SARS-CoV-2
crystal structure
macrodomain
Journal
IUCrJ
ISSN: 2052-2525
Titre abrégé: IUCrJ
Pays: England
ID NLM: 101623101
Informations de publication
Date de publication:
01 Sep 2020
01 Sep 2020
Historique:
received:
22
05
2020
accepted:
15
07
2020
entrez:
17
9
2020
pubmed:
18
9
2020
medline:
18
9
2020
Statut:
epublish
Résumé
Among 15 nonstructural proteins (Nsps), the newly emerging Severe Acute Respiratory Syndrome coronavirus 2 (SARS-CoV-2) encodes a large, multidomain Nsp3. One of its units is the ADP-ribose phosphatase domain (ADRP; also known as the macrodomain, MacroD), which is believed to interfere with the host immune response. Such a function appears to be linked to the ability of the protein to remove ADP-ribose from ADP-ribosylated proteins and RNA, yet the precise role and molecular targets of the enzyme remain unknown. Here, five high-resolution (1.07-2.01 Å) crystal structures corresponding to the apo form of the protein and its complexes with 2-(
Identifiants
pubmed: 32939273
doi: 10.1107/S2052252520009653
pii: lz5040
pmc: PMC7467174
doi:
Types de publication
Journal Article
Langues
eng
Pagination
814-824Informations de copyright
© Karolina Michalska et al. 2020.
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