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Article

Structural and functional analyses of the severe acute respiratory syndrome coronavirus endoribonuclease Nsp15.

The Journal of biological chemistry - 8 Feb 2008

Bhardwaj Kanchan, Palaninathan Satheesh, Alcantara Joanna Maria Ortiz, Li Yi Lillian, Guarino Linda, Sacchettini James C, Kao C Cheng

Abstract excerpt

The severe acute respiratory syndrome (SARS) coronavirus encodes several RNA-processing enzymes that are unusual for RNA viruses, including Nsp15 (nonstructural protein 15), a hexameric endoribonuclease that preferentially cleaves 3' of uridines. We solved the structure of a catalytically inactive mutant version of Nsp15, which was crystallized as a hexamer. The structure contains unreported flexibility in the...

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Identifiers

PMID: 18045871
DOI: 10.1074/jbc.M708375200
PMCID: PMC8740563

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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