2bmf
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(New page: 200px<br /><applet load="2bmf" size="350" color="white" frame="true" align="right" spinBox="true" caption="2bmf, resolution 2.41Å" /> '''DENGUE VIRUS RNA HEL...)
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Revision as of 16:27, 29 January 2008
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DENGUE VIRUS RNA HELICASE AT 2.4A
Overview
Dengue fever is an important emerging public health concern, with several, million viral infections occurring annually, for which no effective, therapy currently exists. The NS3 protein from Dengue virus is a, multifunctional protein of 69 kDa, endowed with protease, helicase, and, nucleoside 5'-triphosphatase (NTPase) activities. Thus, NS3 plays an, important role in viral replication and represents a very interesting, target for the development of specific antiviral inhibitors. We present, the structure of an enzymatically active fragment of the Dengue virus, NTPase/helicase catalytic domain to 2.4 A resolution. The structure is, composed of three domains, displays an asymmetric distribution of charges, on its surface, and contains a tunnel large enough to accommodate, single-stranded RNA. Its C-terminal domain adopts a new fold compared to, the NS3 helicase of hepatitis C virus, which has interesting implications, for the evolution of the Flaviviridae replication complex. A bound sulfate, ion reveals residues involved in the metal-dependent NTPase catalytic, mechanism. Comparison with the NS3 hepatitis C virus helicase complexed to, single-stranded DNA would place the 3' single-stranded tail of a nucleic, acid duplex in the tunnel that runs across the basic face of the protein., A possible model for the unwinding mechanism is proposed.
About this Structure
2BMF is a Single protein structure of sequence from Dengue virus type 3. Full crystallographic information is available from OCA.
Reference
Structure of the Dengue virus helicase/nucleoside triphosphatase catalytic domain at a resolution of 2.4 A., Xu T, Sampath A, Chao A, Wen D, Nanao M, Chene P, Vasudevan SG, Lescar J, J Virol. 2005 Aug;79(16):10278-88. PMID:16051821
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