NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains
Poly(ADP-ribose) polymerases (PARPs) catalyse ADP-ribose posttranslational modifications using NAD+ as a substrate. Here, the authors present the crystal structure of PARP-1 bound to the non-hydrolyzable NAD+ analog BAD and provide insights into the mechanism of PARP-1 allosteric regulation.
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2018-02-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-018-03234-8 |
| _version_ | 1818835069682319360 |
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| author | Marie-France Langelier Levani Zandarashvili Pedro M. Aguiar Ben E. Black John M. Pascal |
| author_facet | Marie-France Langelier Levani Zandarashvili Pedro M. Aguiar Ben E. Black John M. Pascal |
| author_sort | Marie-France Langelier |
| collection | DOAJ |
| description | Poly(ADP-ribose) polymerases (PARPs) catalyse ADP-ribose posttranslational modifications using NAD+ as a substrate. Here, the authors present the crystal structure of PARP-1 bound to the non-hydrolyzable NAD+ analog BAD and provide insights into the mechanism of PARP-1 allosteric regulation. |
| first_indexed | 2024-12-19T02:44:51Z |
| format | Article |
| id | doaj.art-86fcef598c794822b2da2e8ca622e51d |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-19T02:44:51Z |
| publishDate | 2018-02-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-86fcef598c794822b2da2e8ca622e51d2022-12-21T20:38:59ZengNature PortfolioNature Communications2041-17232018-02-019111310.1038/s41467-018-03234-8NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domainsMarie-France Langelier0Levani Zandarashvili1Pedro M. Aguiar2Ben E. Black3John M. Pascal4Department of Biochemistry and Molecular Medicine, Université de MontréalDepartment of Biochemistry and Biophysics, Perelman School of Medicine, University of PennsylvaniaDepartment of Chemistry, Université de MontréalDepartment of Biochemistry and Biophysics, Perelman School of Medicine, University of PennsylvaniaDepartment of Biochemistry and Molecular Medicine, Université de MontréalPoly(ADP-ribose) polymerases (PARPs) catalyse ADP-ribose posttranslational modifications using NAD+ as a substrate. Here, the authors present the crystal structure of PARP-1 bound to the non-hydrolyzable NAD+ analog BAD and provide insights into the mechanism of PARP-1 allosteric regulation.https://doi.org/10.1038/s41467-018-03234-8 |
| spellingShingle | Marie-France Langelier Levani Zandarashvili Pedro M. Aguiar Ben E. Black John M. Pascal NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains Nature Communications |
| title | NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains |
| title_full | NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains |
| title_fullStr | NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains |
| title_full_unstemmed | NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains |
| title_short | NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains |
| title_sort | nad analog reveals parp 1 substrate blocking mechanism and allosteric communication from catalytic center to dna binding domains |
| url | https://doi.org/10.1038/s41467-018-03234-8 |
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