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Domain Organization of Vaccinia Virus Helicase-Primase D5.

Stephanie HutinWai Li LingAdam RoundGregory EffantinStefan ReichFrédéric IseniNicolas TarbouriechGuy SchoehnWim Pascal Burmeister
Published in: Journal of virology (2016)
Since the beginning of the 1980s, research on the vaccinia virus replication mechanism has basically stalled due to the absence of structural information. As a result, this important class of pathogens is less well understood than most other viruses. This lack of information concerns in general viruses of the NCLDV clade, which use a superfamily 3 helicase for replication, as do poxviruses. Here we provide for the first time information about the domain structure and DNA-binding activity of D5, the poxvirus helicase-primase. This result not only refines the current model of the poxvirus replication fork but also will lead in the long run to a structural basis for antiviral drug design.
Keyphrases
  • dna binding
  • structural basis
  • health information
  • transcription factor
  • emergency department
  • healthcare
  • antimicrobial resistance
  • electronic health record
  • genome wide identification