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'''Dengue NS5 Protein'''<StructureSection load='2j7w' size='500' side='right' caption='NS5 polymerase (PDB entry [[2j7w]])' scene=''>The NS5 protein is a 900-residue peptide, which contains a methyltransferase domain. This protein plays an important role in the Dengue virus replication. The protein not only functions as a methyltransferase, but also as a RNA polymerase. The NS5 protein also contains guanylyltransferase activities, which, along with methyltransferase, help protect the viral genome and create efficient protein translation.
'''Dengue NS5 Protein'''<StructureSection load='2j7w' size='500' side='right' caption='NS5 polymerase (PDB entry [[2j7w]])' scene=''>The NS5 protein is a 900-residue peptide, which contains a methyltransferase domain. This protein plays an important role in the Dengue virus replication. The protein not only functions as a methyltransferase, but also as a RNA polymerase. The NS5 protein also contains guanylyltransferase activities, which, along with methyltransferase, help protect the viral genome and create efficient protein translation.
There are four serotypes of the Dengue virus, and the NS5 protein is most prominent in the Dengue-2-serotype, helping it with its pathogenesis.
There are four serotypes of the Dengue virus, and the NS5 protein is most prominent in the Dengue-2-serotype, helping it with its pathogenesis.
Dengue-2 NS5 contains an also has an <scene name='56/565763/Sah/4'>active site</scene> which is considered a "S-adenosyl methionine-dependent methyltransferase fold" structure. The S-adenosyl methionine ligand is methylated in the methyltransferase domain, creating S-adenosyl-l-homocysteine (<scene name='56/565763/Sah/5'>SAH</scene>)as a by-product.  
Dengue-2 NS5 contains an also has an <scene name='56/565763/Sah/4'>active site</scene> which is considered a "S-adenosyl methionine-dependent methyltransferase fold" structure. The S-adenosyl methionine (SAM) ligand is methylated in the methyltransferase domain, creating S-adenosyl-l-homocysteine (<scene name='56/565763/Sah/5'>SAH</scene>)as a by-product. The SAM and SAH are useful in aiding in the folding of the active site.
In the NS5 protein, there is another binding site for GTP. This binding of GTP is done in the N-terminal domain on the protein. The <scene name='56/565763/Active_site_gtp/3'>GTP in the binding site</scene> is what allows the Dengue-2-methyltransferase to complete its functions; these functions include translation, transcription and replication processes.</StructureSection>  
In the NS5 protein, there is another binding site for GTP. This binding of GTP is done in the N-terminal domain on the protein. The <scene name='56/565763/Active_site_gtp/3'>GTP in the binding site</scene> is what allows the Dengue-2-methyltransferase to complete its functions; these functions include translation, transcription and replication processes.</StructureSection>  


'''Dengue NS3/NS2B Protein'''<StructureSection load='2vbc' size='500' side='right' caption='Structure of protease and helicase (PDB entry [[2vbc]])' scene=''>The NS3 protease is a serine protease that can also function as a RNA helicase and RTPase/NTPase. The enzymatic function of this protease is important for the Dengue virus to replicate. This enzyme of the virus is also a potential target for vaccines and antiviral drugs.  
'''Dengue NS3/NS2B Protein'''<StructureSection load='2vbc' size='500' side='right' caption='Structure of protease and helicase (PDB entry [[2vbc]])' scene=''>The NS3 protease is a serine protease that can also function as a RNA helicase and RTPase/NTPase. The enzymatic function of this protease is important for the Dengue virus to replicate. This enzyme of the virus is also a potential target for vaccines and antiviral drugs.  
The catalytic triad <scene name='56/565763/Ns2b/3'>(His-51, Asp-75 and Ser-135)</scene>, is found between these two β-barrels, and its activity is dependent on the presence of the <scene name='56/565763/Ns2b/5'>NS2B</scene>. This cofactor wraps around the NS3 protease domain and becomes part of the active site. The NS2B cofactor is critical for proteolytic activation of the NS3 protease. The NS3 protease is made up of an extensive network of hydrogen bond and hydrophobic interaction, making it very rigid. NS2B is also important in contributing to substrate binding. This implies that the NS2B cofactor acts as an enzyme activator as well as being directly involved in substrate binding/interactions.</StructureSection>
The catalytic triad <scene name='56/565763/Ns2b/3'>(His-51, Asp-75 and Ser-135)</scene>, is found between these two β-barrels, and its activity is dependent on the presence of the <scene name='56/565763/Ns2b/6'>NS2B</scene>. This cofactor then wraps around the NS3 protease domain and becomes part of the active site. The NS2B cofactor is critical for proteolytic activation of the NS3 protease. The NS3 protease is made up of an extensive network of hydrogen bond and hydrophobic interaction, making it very rigid. NS2B is also important in contributing to substrate binding. This implies that NS2B acts as an enzyme activator as well as being directly involved in substrate binding/interactions.</StructureSection>




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[[Category: Icosahedral virus]]
[[Category: Icosahedral virus]]
[[Category: Virus]]
[[Category: Virus]]
== Headline text ==

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Sunjeet Virdi