Conformational flexibility of the dengue virus RNA-Dependent RNA polymerase revealed by a complex with an inhibitor

Christian G. Noble, Siew Pheng Lim, Yen Liang Chen, Chong Wai Liew, Lijian Yap, Julien Lescar, Pei Yong Shi

Research output: Contribution to journalArticlepeer-review

68 Scopus citations

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 languageEnglish (US)
Pages (from-to)5291-5295
Number of pages5
JournalJournal of virology
Volume87
Issue number9
DOIs
StatePublished - May 2013

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

Fingerprint Dive into the research topics of 'Conformational flexibility of the dengue virus RNA-Dependent RNA polymerase revealed by a complex with an inhibitor'. Together they form a unique fingerprint.

Cite this