The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Structural and Functional Basis for ADP-Ribose and Poly(ADP-Ribose) Binding by Viral Macro Domains
Open accessAbstract
Macro domains constitute a protein module family found associated with specific histones and proteins involved in chromatin metabolism. In addition, a small number of animal RNA viruses, such as corona- and toroviruses, alphaviruses, and hepatitis E virus, encode macro domains for which, however, structural and functional information is extremely limited. Here, we characterized the macro domains from hepatitis E virus, Semliki Forest virus, and severe acute respiratory syndrome coronavirus (SARS-CoV). The crystal structure of the SARS-CoV macro domain was determined at 1.8-Å resolution in complex with ADP-ribose. Information derived from structural, mutational, and sequence analyses suggests a close phylogenetic and, most probably, functional relationship between viral and cellular macro domain homologs. The data revealed that viral macro domains have relatively poor ADP-ribose 1"-phosphohydrolase activities (which were previously proposed to be their biologically relevant function) but bind efficiently free and poly(ADP-ribose) polymerase 1-bound poly(ADP-ribose) in vitro. Collectively, these results suggest to further evaluate the role of viral macro domains in host response to viral infection.
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Cites
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
Cited by
Báez-Santos, Y. M., St. John, S. E., & Mesecar, A. D. (2015) · Antiviral Research · doi:10.1016/j.antiviral.2014.12.015 · Cited by 854
PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes
Gupte, R., Liu, Z., & Kraus, W. L. (2017) · Genes & Development · doi:10.1101/gad.291518.116 · Cited by 681
“Interestingly, macrodomain-containing proteins have also been identified in a variety of virus families, including the Coronaviridae, Togaviridae, and Hepeviridae GENES & DEVELOPMENT 111 (Table 1; Egloff et al. 2006;Malet et al. 2009; Li et al. 2016).”
BackgroundHassa, P. (2008) · Frontiers in Bioscience · doi:10.2741/2909 · Cited by 584
Gagné, J.-P., Isabelle, M., Lo, K. S., Bourassa, S., Hendzel, M. J., Dawson, V. L., Dawson, T. M., & Poirier, G. G. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn771 · Cited by 414
Drug Development and Medicinal Chemistry Efforts toward SARS‐Coronavirus and Covid‐19 Therapeutics
Ghosh, A. K., Brindisi, M., Shahabi, D., Chapman, M. E., & Mesecar, A. D. (2020) · ChemMedChem · doi:10.1002/cmdc.202000223 · Cited by 306
Metadata
- Authors
- Egloff, M.-P., Malet, H., Putics, A., Heinonen, M., Dutartre, H., Frangeul, A., Gruez, A., Campanacci, V., Cambillau, C., Ziebuhr, J., Ahola, T., & Canard, B.
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 2006-09
- Volume
- 80
- Issue
- 17
- Pages
- 8493-8502
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- OpenAlex
- W2163279093
- Cited by
- 243
- References
- 1
- FWCI
- 9.33
- Type
- journal article
- Language
- en
- Open access
- green
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- The paper
- Egloff, M.-P., Malet, H., Putics, A., Heinonen, M., Dutartre, H., Frangeul, A., Gruez, A., Campanacci, V., Cambillau, C., Ziebuhr, J., Ahola, T., & Canard, B. (2006). Structural and Functional Basis for ADP-Ribose and Poly(ADP-Ribose) Binding by Viral Macro Domains. Journal of Virology. https://doi.org/10.1128/jvi.00713-06
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