dc.contributor.authorXu, Tingen_US
dc.date.accessioned2008-09-17T11:42:05Z
dc.date.accessioned2017-07-23T08:42:07Z
dc.date.available2008-09-17T11:42:05Z
dc.date.available2017-07-23T08:42:07Z
dc.date.copyright2007en_US
dc.date.issued2007
dc.identifier.citationXu, T. (2007). Structure of the dengue virus helicase/nucleoside triphosphatase catalytic domain. Doctoral thesis, Nanyang Technological University, Singapore.
dc.identifier.urihttp://hdl.handle.net/10356/6575
dc.description.abstractInfectious diseases caused by flaviviruses are important emerging public health concerns and new vaccines and therapeutics are urgently needed. The NS3 protein from flavivirus is a multifunctional protein with protease, helicase and nucleoside 5' triphosphatase activities (NTPase). Thus, NS3 plays a crucial role in viral replication and represents an interesting target for the development of specific antiviral inhibitors. This thesis reported the structure of an enzymatically active fragment of the dengue virus NTPase/ helicase C-terminal catalytic domain. The structure is composed of three domains, bears an asymmetric distribution of charges and comprises a tunnel large enough to accommodate single strand RNA. A concave face formed by domains 2 and 3 is proposed to bind a nucleic acid duplex substrate. Comparison of the various copies of dengue and yellow fever virus NS3 NTPase/helicase catalytic domains reveals mobile regions of the enzyme. Such dynamic behaviour is likely to be coupled with directional translocation along the single strand nucleic acid substrate during strand separation.en_US
dc.rightsNanyang Technological Universityen_US
dc.subjectDRNTU::Science::Biological sciencesen_US
dc.titleStructure of the dengue virus helicase/nucleoside triphosphatase catalytic domainen_US
dc.typeThesisen_US
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.contributor.supervisorJulien Lescaren_US
dc.description.degreeDOCTOR OF PHILOSOPHY (SBS)en_US


Files in this item

FilesSizeFormatView
SBS-THESES_21.pdf7.714Mbapplication/pdfView/Open

This item appears in the following Collection(s)

Show simple item record