ArticleProtein science : a publication of the Protein Society2009
Crystal structures of the X-domains of a Group-1 and a Group-3 coronavirus reveal that ADP-ribose-binding may not be a conserved property.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 41 citations in OpenAlex.
- Recombinant infectious bronchitis virus containing mutations in non-structural proteins 10, 14, 15, and 16 and within the macrodomain provides complete protection against homologous challenge.Journal of virology · 2025Article
- Crystal structure and biochemical activity of the macrodomain from rubella virus p150.Journal of virology · 2024Article
- Drug similarity and structure-based screening of medicinal compounds to target macrodomain-I from SARS-CoV-2 to rescue the host immune system: a molecular dynamics study.Journal of biomolecular structure & dynamics · 2022Article
- ADP-ribose and analogues bound to the deMARylating macrodomain from the bat coronavirus HKU4.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Crystal structures of SARS-CoV-2 ADP-ribose phosphatase: from the apo form to ligand complexes.IUCrJ · 2020Article
- Article
- Deciphering the Nucleotide and RNA Binding Selectivity of the Mayaro Virus Macro Domain.Journal of molecular biology · 2019Article
- The ADRP domain from a virulent strain of infectious bronchitis virus is not sufficient to confer a pathogenic phenotype to the attenuated Beaudette strain.The Journal of general virology · 2018Article
- Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein.Antiviral research · 2018Review
- Structural basis for dimerization and RNA binding of avian infectious bronchitis virus nsp9.Protein science : a publication of the Protein Society · 2017Article
- Structural and functional analysis ofOpen biology · 2017Article
- The conserved macrodomains of the non-structural proteins of Chikungunya virus and other pathogenic positive strand RNA viruses function as mono-ADP-ribosylhydrolases.Scientific reports · 2017Article
- The macro domain as fusion tag for carrier-driven crystallization.Protein science : a publication of the Protein Society · 2017Article
- Bioinformatics and functional analyses of coronavirus nonstructural proteins involved in the formation of replicative organelles.Antiviral research · 2016Review
- Macro Domain from Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Is an Efficient ADP-ribose Binding Module: CRYSTAL STRUCTURE AND BIOCHEMICAL STUDIES.The Journal of biological chemistry · 2016Article
- X-ray Structural and Functional Studies of the Three Tandemly Linked Domains of Non-structural Protein 3 (nsp3) from Murine Hepatitis Virus Reveal Conserved Functions.The Journal of biological chemistry · 2015Article
- Article
- Article
- Reprogramming cellular events by poly(ADP-ribose)-binding proteins.Molecular aspects of medicine · 2013Review
- From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses.Antiviral research · 2013Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The polyproteins of coronaviruses are cleaved by viral proteases into at least 15 nonstructural proteins (Nsps). Consisting of five domains, Nsp3 is the largest of these (180-210 kDa). Among these domains, the so-called X-domain is believed to act as ADP-ribose-1''-phosphate phosphatase or to bind poly(ADP-ribose). However, here we show that the X-domain of Infectious Bronchitis Virus (strain Beaudette), a Group-3 coronavirus, fails to bind ADP-ribose. This is explained on the basis of the crystal structure of the protein, determined at two different pH values. For comparison, we also describe the crystal structure of the homologous X-domain from Human Coronavirus 229E, a Group-1 coronavirus, which does bind ADP-ribose.
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