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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
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 po...
| Autores principales: | , , , , , |
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| Formato: | Texto |
| Lenguaje: | English |
| Publicado: |
Wiley Subscription Services, Inc., A Wiley Company
2009
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2708038/ https://www.ncbi.nlm.nih.gov/pubmed/19177346 http://dx.doi.org/10.1002/pro.15 |