期刊
JOURNAL OF VIROLOGY
卷 87, 期 9, 页码 5291-5295出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.00045-13
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- BMRC [0912219/599]
We report a highly reproducible method to crystallize the RNA-dependent RNA polymerase (RdRp) domain of dengue virus serotype 3 (DENV-3), allowing structure refinement to a 1.79-angstrom resolution and revealing amino acids not seen previously. We also present a DENV-3 polymerase/inhibitor cocrystal structure at a 2.1-angstrom resolution. The inhibitor binds to the RdRp as a dimer and causes conformational changes in the protein. The improved crystallization conditions and new structural information should accelerate structure-based drug discovery.
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