2JQM
Yellow Fever Envelope Protein Domain III NMR Structure (S288-K398)
Summary for 2JQM
| Entry DOI | 10.2210/pdb2jqm/pdb |
| Descriptor | Envelope protein E (1 entity in total) |
| Functional Keywords | yellow fever envelope protein domain iii, asibi strain, transferase |
| Biological source | Yellow fever 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). Non-structural protein 1: Secreted. Non-structural protein 2A-alpha: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Non-structural protein 2A: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side (By similarity). Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side (By similarity). Non-structural protein 4A: Host endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): Q6J3P1 |
| Total number of polymer chains | 1 |
| Total formula weight | 11951.75 |
| Authors | Volk, D.E.,Gandham, S.H.,May, F.J.,Anderson, A.,Barrett, A.D.,Gorenstein, D.G. (deposition date: 2007-06-03, release date: 2008-06-10, Last modification date: 2024-10-30) |
| Primary citation | Volk, D.E.,May, F.J.,Gandham, S.H.,Anderson, A.,Von Lindern, J.J.,Beasley, D.W.,Barrett, A.D.,Gorenstein, D.G. Structure of yellow fever virus envelope protein domain III. Virology, 394:12-18, 2009 Cited by PubMed Abstract: The structure of recombinant domain III of the envelope protein (rED3) of yellow fever virus (YFV), containing the major neutralization site, was determined using NMR spectroscopy. The amino acid sequence and structure of the YFV-rED3 shows differences from ED3s of other mosquito-borne flaviviruses; in particular, the partially surface-exposed BC loop where methionine-304 and valine-324 were identified as being critical for the structure of the loop. Variations in the structure and surface chemistry of ED3 between flaviviruses affect neutralization sites and may affect host cell receptor interactions and play a role in the observed variations in viral pathogenesis and tissue tropism. PubMed: 19818466DOI: 10.1016/j.virol.2009.09.001 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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