1z66
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(New page: 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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Revision as of 05:08, 21 November 2007
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NMR solution structure of domain III of E-protein of tick-borne Langat flavivirus (no RDC restraints)
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.
About this Structure
1Z66 is a Single protein structure of sequence from Langat virus. Full crystallographic information is available from OCA.
Reference
NMR solution structure and backbone dynamics of domain III of the E protein of tick-borne Langat flavivirus suggests a potential site for molecular recognition., Mukherjee M, Dutta K, White MA, Cowburn D, Fox RO, Protein Sci. 2006 Jun;15(6):1342-55. PMID:16731969
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