Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix
The viral Protein Kinase-1 (PK-1) phosphorylates the regulatory protein p6.9, which facilitates baculoviral genome release. Here, the authors combine X-ray crystallography with biophysical and biochemical analyses as well as molecular dynamics simulations to characterize Cydia pomenella granulovirus...
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Nature Portfolio
2021
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oai:doaj.org-article:68962591ebc346e3865840990c4f686b2021-12-02T13:30:15ZGranulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix10.1038/s41467-021-21191-72041-1723https://doaj.org/article/68962591ebc346e3865840990c4f686b2021-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21191-7https://doaj.org/toc/2041-1723The viral Protein Kinase-1 (PK-1) phosphorylates the regulatory protein p6.9, which facilitates baculoviral genome release. Here, the authors combine X-ray crystallography with biophysical and biochemical analyses as well as molecular dynamics simulations to characterize Cydia pomenella granulovirus PK-1, which forms a dimer with a parallel side-to-side arrangement of the kinase domains and furthermore, they provide insights into its catalytic mechanism and evolutionary relationships with other kinases.Michael R. OliverChristopher R. HorneSafal ShresthaJeremy R. KeownLung-Yu LiangSamuel N. YoungJarrod J. SandowAndrew I. WebbDavid C. GoldstoneIsabelle S. LucetNatarajan KannanPeter MetcalfJames M. MurphyNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-11 (2021) |
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| topic |
Science Q |
| spellingShingle |
Science Q Michael R. Oliver Christopher R. Horne Safal Shrestha Jeremy R. Keown Lung-Yu Liang Samuel N. Young Jarrod J. Sandow Andrew I. Webb David C. Goldstone Isabelle S. Lucet Natarajan Kannan Peter Metcalf James M. Murphy Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix |
| description |
The viral Protein Kinase-1 (PK-1) phosphorylates the regulatory protein p6.9, which facilitates baculoviral genome release. Here, the authors combine X-ray crystallography with biophysical and biochemical analyses as well as molecular dynamics simulations to characterize Cydia pomenella granulovirus PK-1, which forms a dimer with a parallel side-to-side arrangement of the kinase domains and furthermore, they provide insights into its catalytic mechanism and evolutionary relationships with other kinases. |
| format |
article |
| author |
Michael R. Oliver Christopher R. Horne Safal Shrestha Jeremy R. Keown Lung-Yu Liang Samuel N. Young Jarrod J. Sandow Andrew I. Webb David C. Goldstone Isabelle S. Lucet Natarajan Kannan Peter Metcalf James M. Murphy |
| author_facet |
Michael R. Oliver Christopher R. Horne Safal Shrestha Jeremy R. Keown Lung-Yu Liang Samuel N. Young Jarrod J. Sandow Andrew I. Webb David C. Goldstone Isabelle S. Lucet Natarajan Kannan Peter Metcalf James M. Murphy |
| author_sort |
Michael R. Oliver |
| title |
Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix |
| title_short |
Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix |
| title_full |
Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix |
| title_fullStr |
Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix |
| title_full_unstemmed |
Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix |
| title_sort |
granulovirus pk-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αc helix |
| publisher |
Nature Portfolio |
| publishDate |
2021 |
| url |
https://doaj.org/article/68962591ebc346e3865840990c4f686b |
| work_keys_str_mv |
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