Abstract
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-å resolution and revealing amino acids not seen previously. We also present a DENV-3 polymerase/inhibitor cocrystal structure at a 2.1-å 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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 5291-5295 |
| Number of pages | 5 |
| Journal | Journal of virology |
| Volume | 87 |
| Issue number | 9 |
| DOIs | |
| State | Published - May 2013 |
ASJC Scopus subject areas
- Microbiology
- Immunology
- Insect Science
- Virology