1z66: Difference between revisions

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New page: left|200px<br /><applet load="1z66" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z66" /> '''NMR solution structure of domain III of E-pr...
 
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[[Image:1z66.gif|left|200px]]<br /><applet load="1z66" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1z66.gif|left|200px]]<br /><applet load="1z66" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1z66" />
caption="1z66" />
'''NMR solution structure of domain III of E-protein of tick-borne Langat flavivirus (no RDC restraints)'''<br />
'''NMR solution structure of domain III of E-protein of tick-borne Langat flavivirus (no RDC restraints)'''<br />


==Overview==
==Overview==
Flaviviruses cause many human diseases, including dengue fever, yellow, fever, West Nile viral encephalitis, and hemorrhagic fevers, and are, transmitted to their vertebrate hosts by infected mosquitoes and ticks., Domain III of the envelope protein (E-D3) is considered to be the primary, viral determinant involved in the virus-host-cell receptor interaction, and thus represents an excellent target for antiviral drug development., Langat (LGT) virus is a naturally attenuated BSL-2 TBE virus and is a, model for the pathogenic BSL-3 and BSL-4 viruses in the serogroup. We have, determined the solution structure of LGT-E-D3 using heteronuclear NMR, spectroscopy. The backbone dynamics of LGT-E-D3 have been investigated, using 15N relaxation measurements. A detailed analysis of the solution, structure and dynamics of LGT-E-D3 suggests potential residues that could, form a surface for molecular recognition, and thereby represent a target, site for antiviral therapeutics design.
Flaviviruses cause many human diseases, including dengue fever, yellow fever, West Nile viral encephalitis, and hemorrhagic fevers, and are transmitted to their vertebrate hosts by infected mosquitoes and ticks. Domain III of the envelope protein (E-D3) is considered to be the primary viral determinant involved in the virus-host-cell receptor interaction, and thus represents an excellent target for antiviral drug development. Langat (LGT) virus is a naturally attenuated BSL-2 TBE virus and is a model for the pathogenic BSL-3 and BSL-4 viruses in the serogroup. We have determined the solution structure of LGT-E-D3 using heteronuclear NMR spectroscopy. The backbone dynamics of LGT-E-D3 have been investigated using 15N relaxation measurements. A detailed analysis of the solution structure and dynamics of LGT-E-D3 suggests potential residues that could form a surface for molecular recognition, and thereby represent a target site for antiviral therapeutics design.


==About this Structure==
==About this Structure==
1Z66 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Langat_virus Langat virus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z66 OCA].  
1Z66 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Langat_virus Langat virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z66 OCA].  


==Reference==
==Reference==
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[[Category: Cowburn, D.]]
[[Category: Cowburn, D.]]
[[Category: Dutta, K.]]
[[Category: Dutta, K.]]
[[Category: Fox, R.O.]]
[[Category: Fox, R O.]]
[[Category: Mukherjee, M.]]
[[Category: Mukherjee, M.]]
[[Category: White, M.A.]]
[[Category: White, M A.]]
[[Category: viral protein]]
[[Category: viral protein]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:25 2008''