Structural highlights
Function
[Q6DLV0_9FLAV] Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).[SAAS:SAAS000336_004_099774]
Publication Abstract from PubMed
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 1.79 A resolution and revealing amino acids not seen previously. We also present a DENV-3 polymerase/inhibitor co-crystal structure at 2.1 A 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.
Conformational flexibility of the dengue virus RNA-dependent RNA polymerase revealed by a complex with an inhibitor.,Noble CG, Lim SP, Chen YL, Liew CW, Yap L, Lescar J, Shi PY J Virol. 2013 Feb 13. PMID:23408636[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Noble CG, Lim SP, Chen YL, Liew CW, Yap L, Lescar J, Shi PY. Conformational flexibility of the dengue virus RNA-dependent RNA polymerase revealed by a complex with an inhibitor. J Virol. 2013 Feb 13. PMID:23408636 doi:10.1128/JVI.00045-13
