The flavivirus precursor membrane-envelope protein complex: Structure and maturation

Science

Volumn 319, Issue 5871, 2008, Pages 1830-1834

  Li, Long ^a   Lok, Shee Mei ^a   Yu, I Mei ^a   Zhang, Ying ^a   Kuhn, Richard J ^a   Chen, Jue ^a   Rossmann, Michael G ^a  

^a PURDUE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN E; HETERODIMER; PRECURSOR MEMBRANE PROTEIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN;

CRYSTAL STRUCTURE; DENGUE FEVER; ELECTRON MICROSCOPY; HOST-PATHOGEN INTERACTION; MATURATION; METAMORPHOSIS; PEPTIDE; PH; PROTEIN; RECOMBINATION; VIRUS;

ARTICLE; CONFORMATIONAL TRANSITION; CRYOELECTRON MICROSCOPY; CRYSTAL STRUCTURE; DENSITY; DIMERIZATION; FLAVIVIRUS; HOST CELL; IMAGE ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN PROCESSING; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; VIRUS CELL INTERACTION;

CRYSTALLOGRAPHY, X-RAY; DENGUE VIRUS; DIMERIZATION; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN PRECURSORS; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; VIRAL ENVELOPE PROTEINS; VIRAL MATRIX PROTEINS; VIRUS ASSEMBLY;

DENGUE VIRUS; FLAVIVIRUS;

EID: 41349112506     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1153263     Document Type: Article

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21. Single-letter abbreviations for amino acid residues: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; Y, Tyr.
22. We thank Y. Xiang and W. Zhang for many helpful discussions; S. Kelly and C. Towell for help in the preparation of the manuscript; and the staff at APS GM/CA sector for their help in data collection. The facilities are supported by the U.S. Department of Energy and/or NIH. The work was supported by NIH program project grant AI055672 (R.J.K., M.G.R., J.C.) and National Institute of Allergy and Infectious Diseases Region V Great Lakes Center of Excellence for Biodefense and Emerging Infectious Diseases Research Program award 1-U54-AI-057153 (R.J.K., M.G.R.). The coordinates of the prM-E heterodimer crystal structures at pH 5.5 and 7.0 have been deposited with the Protein Data Bank (accession numbers 3C5X and 3C6E, respectively). The fit of the prM-E heterodimer into the cryoEM reconstruction of the dengue immature virus at neutral pH has been deposited with the RCSB Protein Database (accession number 3C6D).