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3lkw

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Revision as of 20:35, 4 August 2016

Crystal Structure of Dengue Virus 1 NS2B/NS3 protease active site mutant

Structural highlights

3lkw is a 1 chain structure with sequence from Dengue virus 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	3l6p
Gene:	NS2B/NS3 (Dengue virus 1)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[Q9J7C6_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:SAAS026470_004_099774]

Publication Abstract from PubMed

With an estimated 40% of the world population at risk, dengue poses a significant threat to human health, especially in tropical and subtropical regions. Preventative and curative efforts, such as vaccine development and drug discovery, face additional challenges due to the occurrence of four antigenically distinct serotypes of the causative dengue virus (DEN1 to -4). Complex immune responses resulting from repeat assaults by the different serotypes necessitate simultaneous targeting of all forms of the virus. One of the promising targets for drug development is the highly conserved two-component viral protease NS2B-NS3, which plays an essential role in viral replication by processing the viral precursor polyprotein into functional proteins. In this paper, we report the 2.1-A crystal structure of the DEN1 NS2B hydrophilic core (residues 49 to 95) in complex with the NS3 protease domain (residues 1 to 186) carrying an internal deletion in the N terminus (residues 11 to 20). While the overall folds within the protease core are similar to those of DEN2 and DEN4 proteases, the conformation of the cofactor NS2B is dramatically different from those of other flaviviral apoprotease structures. The differences are especially apparent within its C-terminal region, implicated in substrate binding. The structure reveals for the first time serotype-specific structural elements in the dengue virus family, with the reported alternate conformation resulting from a unique metal-binding site within the DEN1 sequence. We also report the identification of a 10-residue stretch within NS3pro that separates the substrate-binding function from the catalytic turnover rate of the enzyme. Implications for broad-spectrum drug discovery are discussed.

Serotype-specific structural differences in the protease-cofactor complexes of the dengue virus family.,Chandramouli S, Joseph JS, Daudenarde S, Gatchalian J, Cornillez-Ty C, Kuhn P J Virol. 2010 Mar;84(6):3059-67. Epub 2009 Dec 30. PMID:20042502^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chandramouli S, Joseph JS, Daudenarde S, Gatchalian J, Cornillez-Ty C, Kuhn P. Serotype-specific structural differences in the protease-cofactor complexes of the dengue virus family. J Virol. 2010 Mar;84(6):3059-67. Epub 2009 Dec 30. PMID:20042502 doi:10.1128/JVI.02044-09

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3lkw"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Dengue Virus 1 NS2B/NS3 protease active site mutant==
 <StructureSection load='3lkw' size='340' side='right' caption='[[3lkw]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3l6p|3l6p]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NS2B/NS3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11053 Dengue virus 1])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lkw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lkw RCSB], [http://www.ebi.ac.uk/pdbsum/3lkw PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lkw OCA], [http://pdbe.org/3lkw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lkw RCSB], [http://www.ebi.ac.uk/pdbsum/3lkw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lkw ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3lkw" style="background-color:#fffaf0;"></div>
 ==See Also==

3lkw

From Proteopedia

Revision as of 20:35, 4 August 2016

Crystal Structure of Dengue Virus 1 NS2B/NS3 protease active site mutant

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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