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New functional domains of human cytomegalovirus pUL89 predicted by sequence analysis and three-dimensional modelling of the catalytic site DEXDc.

Authors
  • Champier, Gaël
  • Hantz, Sébastien
  • Couvreux, Anthony
  • Stuppfler, Stéphanie
  • Mazeron, Marie-Christine
  • Bouaziz, Serge
  • Denis, François
  • Alain, Sophie
Type
Published Article
Journal
Diabetes care
Publication Date
Jan 01, 2007
Volume
12
Issue
2
Pages
217–232
Identifiers
PMID: 17503664
Source
USPC - SET - SVS
License
Unknown

Abstract

To better understand HCMV DNA maturation and the mechanism of action of benzimidazole derivatives, we studied the HCMV pUL89 protein by a genetic approach combined with primary structure analysis. The pUL89 sequence analysis of 25 HCMV strains and counterparts among herpesviruses allowed identification of 12 conserved regions. We also built a three-dimensional model of the pUL89 ATPasic catalytic site, including ATPase motor motifs 1, II and III, that may facilitate the development of future antiviral drugs active against HCMV. Finally, we identified several putative functional domains in pUL89, such as pUL89 zinc finger (pUL89-ZF), DNA cutting sites and portal binding sites, that are probably involved in CMV DNA cleavage and packaging.

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