ArticleProtein science : a publication of the Protein Society2017
SARS-unique fold in the Rousettus bat coronavirus HKU9.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 7 citations in OpenAlex.
- Study of key residues in MERS-CoV and SARS-CoV-2 main proteases for resistance against clinically applied inhibitors nirmatrelvir and ensitrelvir.Npj viruses · 2024Article
- Article
- Evolution, Ecology, and Zoonotic Transmission of Betacoronaviruses: A Review.Frontiers in veterinary science · 2021Review
- An Overview of the Crystallized Structures of the SARS-CoV-2.The protein journal · 2020Review
- Structure of the SARS-Unique Domain C From the Bat Coronavirus HKU4.Natural product communications · 2019Article
- Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein.Antiviral research · 2018Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The coronavirus nonstructural protein 3 (nsp3) is a multifunctional protein that comprises multiple structural domains. This protein assists viral polyprotein cleavage, host immune interference, and may play other roles in genome replication or transcription. Here, we report the solution NMR structure of a protein from the "SARS-unique region" of the bat coronavirus HKU9. The protein contains a frataxin fold or double-wing motif, which is an α + β fold that is associated with protein/protein interactions, DNA binding, and metal ion binding. High structural similarity to the human severe acute respiratory syndrome (SARS) coronavirus nsp3 is present. A possible functional site that is conserved among some betacoronaviruses has been identified using bioinformatics and biochemical analyses. This structure provides strong experimental support for the recent proposal advanced by us and others that the "SARS-unique" region is not unique to the human SARS virus, but is conserved among several different phylogenetic groups of coronaviruses and provides essential functions.
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Registered trials
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