From Proteopedia
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| - | [[Image:2vbc.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2vbc.png|left|200px]] |
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| | {{STRUCTURE_2vbc| PDB=2vbc | SCENE= }} | | {{STRUCTURE_2vbc| PDB=2vbc | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF THE NS3 PROTEASE-HELICASE FROM DENGUE VIRUS'''
| + | ===CRYSTAL STRUCTURE OF THE NS3 PROTEASE-HELICASE FROM DENGUE VIRUS=== |
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| - | ==Overview==
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| - | Several flaviviruses are important human pathogens, including dengue virus, a disease against which neither a vaccine nor specific antiviral therapies currently exist. During infection, the flavivirus RNA genome is translated into a polyprotein, which is cleaved into several components. Nonstructural protein 3 (NS3) carries out enzymatic reactions essential for viral replication, including proteolysis of the polyprotein through its serine protease N-terminal domain, with a segment of 40 residues from the NS2B protein acting as a cofactor. The ATPase/helicase domain is located at the C terminus of NS3. Atomic structures are available for these domains separately, but a molecular view of the full-length flavivirus NS3 polypeptide is still lacking. We report a crystallographic structure of a complete NS3 molecule fused to 18 residues of the NS2B cofactor at a resolution of 3.15 A. The relative orientation between the protease and helicase domains is drastically different than the single-chain NS3-NS4A molecule from hepatitis C virus, which was caught in the act of cis cleavage at the NS3-NS4A junction. Here, the protease domain sits beneath the ATP binding site, giving the molecule an elongated shape. The domain arrangement found in the crystal structure fits nicely into an envelope determined ab initio using small-angle X-ray scattering experiments in solution, suggesting a stable molecular conformation. We propose that a basic patch located at the surface of the protease domain increases the affinity for nucleotides and could also participate in RNA binding, explaining the higher unwinding activity of the full-length enzyme compared to that of the isolated helicase domain.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17942558}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17942558 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17942558}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Rna replication]] | | [[Category: Rna replication]] |
| | [[Category: Transmembrane]] | | [[Category: Transmembrane]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:32:50 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 23 07:58:35 2008'' |
Revision as of 04:58, 23 July 2008
Template:STRUCTURE 2vbc
CRYSTAL STRUCTURE OF THE NS3 PROTEASE-HELICASE FROM DENGUE VIRUS
Template:ABSTRACT PUBMED 17942558
About this Structure
2VBC is a Protein complex structure of sequences from Dengue virus 4. Full crystallographic information is available from OCA.
Reference
Crystal structure of the NS3 protease-helicase from dengue virus., Luo D, Xu T, Hunke C, Gruber G, Vasudevan SG, Lescar J, J Virol. 2008 Jan;82(1):173-83. Epub 2007 Oct 17. PMID:17942558
Page seeded by OCA on Wed Jul 23 07:58:35 2008
