Identification of a binding pocket of letermovir in the terminase subunit pUL56 of human cytomegalovirus.

ABSTRACT: A key step in replication of human cytomegalovirus (HCMV) is the generation and packaging of unit-length genomes into preformed capsids. The enzymes involved in this process are viral terminases. The HCMV terminase consists of two subunits, the ATPase pUL56 and the nuclease pUL89. A potential third component, pUL51, has been proposed. Letermovir is the first terminase inhibitor available for HCMV prophylaxis to allogenic hematopoietic stem cell recipients. However, mutations in the HCMV terminase subunit pUL56 and, to a lesser extent, in pUL89 or pUL51 lead to resistance. Here we focused on the drug target area in the terminase subunit pUL56. To gain further structural insights into the putative binding site of letermovir, in silico analysis of the structure was performed using Phyre2 and

SUBMITTER: Kmetsch LM 

PROVIDER: S-EPMC11937570 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature