Ontology highlight
ABSTRACT:
SUBMITTER: Zuhlsdorf M
PROVIDER: S-EPMC4498786 | biostudies-literature | 2015 Jul
REPOSITORIES: biostudies-literature
PLoS pathogens 20150710 7
Herpesviruses encode a characteristic serine protease with a unique fold and an active site that comprises the unusual triad Ser-His-His. The protease is essential for viral replication and as such constitutes a promising drug target. In solution, a dynamic equilibrium exists between an inactive monomeric and an active dimeric form of the enzyme, which is believed to play a key regulatory role in the orchestration of proteolysis and capsid assembly. Currently available crystal structures of herp ...[more]