Dataset Information
Motion-corrected micrographs for herpesvirus helicase-primase complex bound to forked DNA with inhibitor Amenamevir
Ontology highlight
ABSTRACT:
SUBMITTER: CI JI LIM
PROVIDER: EMPIAR-13141 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structural basis of herpesvirus helicase-primase inhibition by pritelivir and amenamevir.
Science advances 20251107 45
Widespread herpesvirus infections are associated with various diseases. DNA replication of human herpes simplex virus type 1 (HSV-1) requires a helicase-primase (HP) complex of three core proteins: UL5, UL52, and UL8. This complex unwinds viral DNA and synthesizes primers for DNA replication, making it an attractive antiviral target. Although HP inhibitors pritelivir and amenamevir were identified through screening, their binding mechanisms remain unclear. Here, we report cryo-electron microscop ...[more]