Understanding the unique mechanism of L-FMAU (clevudine) against hepatitis B virus: molecular dynamics studies.
The molecular dynamics simulation of HBV-polymerase.DNA.L-FMAU-TP complex demonstrated that L-FMAU-TP may not serve as a substrate for HBV polymerase because the appropriate binding of L-FMAU-TP to the active site of HBV polymerase may not take place without the unfavorable conformational adjustment, which prevents L-FMAU-TP from being incorporated into the growing viral DNA chain.
Chong
Youhoon
Y
Department of Pharmaceutical and Biomedical Sciences, College of Pharmacy, The University of Georgia, Athens, GA 30602, USA.
Chu
Chung K
CK
D000998:Antiviral Agents / Q000737:chemistry / Q000494:pharmacology*; D001086:Arabinofuranosyluracil / Q000031:analogs & derivatives* / Q000737:chemistry / Q000494:pharmacology*; D001665:Binding Sites; D003198:Computer Simulation; D004261:DNA Replication / Q000187:drug effects; D016208:Databases, Factual; D006515:Hepatitis B virus / Q000187:drug effects* / Q000201:enzymology; D008958:Models, Molecular; D019384:Nucleic Acid Synthesis Inhibitors; D011485:Protein Binding; D011487:Protein Conformation; D014779:Virus Replication / Q000187:drug effects
D000998:Antiviral Agents; D019384:Nucleic Acid Synthesis Inhibitors; D001086:Arabinofuranosyluracil; C034935:clevudine