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Crystal structure of protein tyrosine phosphatase-2 from Cydia pomonella granulovirus
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Huang, Guangmei, Oliver, Michael R., Keown, Jeremy R., Goldstone, David C. and Metcalf, Peter (2019) Crystal structure of protein tyrosine phosphatase-2 from Cydia pomonella granulovirus. Acta Crystallographica Section F Structural Biology Communications, 75 (4). pp. 233-238. doi:10.1107/S2053230X19002322 ISSN 2053-230X.
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Official URL: http://doi.org/10.1107/S2053230X19002322
Abstract
Many viral genomes encode kinase and phosphatase enzymes to manipulate pathways that are controlled by phosphorylation events. The majority of viral phosphatase genes occur in the Baculoviridae and Poxviridae families of large DNA viruses. The corresponding protein sequences belong to four major homology groups, and structures are currently available for only two of these. Here, the first structure from the third group, the protein tyrosine phosphatase-2 (PTP-2) class of viral phosphatases, is described. It is shown that Cydia pomonella granulovirus PTP-2 has the same general fold and active-site architecture as described previously for other phosphatases, in the absence of significant sequence homology. Additionally, it has a novel C-terminal extension in an area corresponding to the interface of dimeric poxvirus phosphatases belonging to the Tyr–Ser protein phosphatase homology group.
Item Type: | Journal Article | ||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||
Journal or Publication Title: | Acta Crystallographica Section F Structural Biology Communications | ||||
Publisher: | International Union of Crystallography | ||||
ISSN: | 2053-230X | ||||
Official Date: | 1 April 2019 | ||||
Dates: |
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Volume: | 75 | ||||
Number: | 4 | ||||
Page Range: | pp. 233-238 | ||||
DOI: | 10.1107/S2053230X19002322 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access |
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