1z66
From Proteopedia
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| - | [[Image:1z66.gif|left|200px]] | + | [[Image:1z66.gif|left|200px]] |
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| - | '''NMR solution structure of domain III of E-protein of tick-borne Langat flavivirus (no RDC restraints)''' | + | {{Structure |
| + | |PDB= 1z66 |SIZE=350|CAPTION= <scene name='initialview01'>1z66</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''NMR solution structure of domain III of E-protein of tick-borne Langat flavivirus (no RDC restraints)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1Z66 is a [ | + | 1Z66 is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16731969 16731969] |
[[Category: Langat virus]] | [[Category: Langat virus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: viral protein]] | [[Category: viral protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:31:35 2008'' |
Revision as of 13:31, 20 March 2008
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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
Page seeded by OCA on Thu Mar 20 15:31:35 2008
