1Z66
NMR solution structure of domain III of E-protein of tick-borne Langat flavivirus (no RDC restraints)
Summary for 1Z66
| Entry DOI | 10.2210/pdb1z66/pdb |
| Related | 1PJW 1S6N 1SVB 1YZO |
| NMR Information | BMRB: 5971 |
| Descriptor | Major envelope protein E (1 entity in total) |
| Functional Keywords | viral protein |
| Biological source | Langat virus |
| Cellular location | Capsid protein C: Virion (Potential). Peptide pr: Secreted (By similarity). Small envelope protein M: Virion membrane; Multi-pass membrane protein (By similarity). Envelope protein E: Virion membrane; Multi- pass membrane protein (By similarity): P29838 |
| Total number of polymer chains | 1 |
| Total formula weight | 10612.12 |
| Authors | Mukherjee, M.,Dutta, K.,White, M.A.,Cowburn, D.,Fox, R.O. (deposition date: 2005-03-21, release date: 2006-03-28, Last modification date: 2024-11-13) |
| Primary citation | Mukherjee, M.,Dutta, K.,White, M.A.,Cowburn, D.,Fox, R.O. 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. Protein Sci., 15:1342-1355, 2006 Cited by PubMed Abstract: 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. PubMed: 16731969DOI: 10.1110/ps.051844006 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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