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Identification of Crucial Hydrogen-Bonding Residues for the Interaction of Herpes Simplex Virus DNA Polymerase Subunits via Peptide Display, Mutational, and Calorimetric Approaches

The catalytic subunit, Pol, of herpes simplex virus DNA polymerase interacts via its extreme C terminus with the processivity subunit, UL42. This interaction is critical for viral replication and thus a potential target for antiviral drug action. To investigate the Pol-binding region on UL42, we eng...

Ausführliche Beschreibung

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Bibliografische Detailangaben
Veröffentlicht in:J Virol
Hauptverfasser: Bridges, Kristie Grove, Chow, Connie S., Coen, Donald M.
Format: Artigo
Sprache:Inglês
Veröffentlicht: American Society for Microbiology (ASM) 2001
Schlagworte:
Online-Zugang:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC114902/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11333878/
https://ncbi.nlm.nih.govhttps://doi.org/10.1128/JVI.75.11.4990-4998.2001
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