Structure of the Uncleaved Human H1 Hemagglutinin from the Extinct 1918 Influenza Virus

Science

Volumn 303, Issue 5665, 2004, Pages 1866-1870

  Stevens, James ^a   Corper, Adam L ^a   Basler, Christopher F ^b   Taubenberger, Jeffery K ^c   Palese, Peter ^b   Wilson, Ian A ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b MOUNT SINAI SCHOOL OF MEDICINE   (United States)

^c ARMED FORCES INSTITUTE OF PATHOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGENS; BIOLOGICAL MEMBRANES; CRYSTAL STRUCTURE; DISEASES; GENES; TISSUE;

PRECURSORS; SURFACE ANTIGENS;

VIRUSES;

HEMAGGLUTININ; HEMAGGLUTININ H1; UNCLASSIFIED DRUG;

INFLUENZA; MEDICINE;

ARTICLE; CRYSTAL STRUCTURE; ENDOSOME; HUMAN; INFLUENZA VIRUS; INTERNALIZATION; MEMBRANE FUSION; PRIORITY JOURNAL; RECEPTOR BINDING; SEROTYPE; VIRUS ACTIVATION; VIRUS ASSEMBLY; VIRUS ENVELOPE; VIRUS INFECTION; VIRUS MORPHOLOGY;

AMINO ACID SEQUENCE; BINDING SITES; CARBOHYDRATE CONFORMATION; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; GLYCOSYLATION; HEMAGGLUTININ GLYCOPROTEINS, INFLUENZA VIRUS; HISTIDINE; HISTORY, 20TH CENTURY; HUMANS; HYDROGEN BONDING; INFLUENZA A VIRUS; INFLUENZA, HUMAN; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, VIRUS; SIALIC ACIDS;

AVES; DNA VIRUSES; INFLUENZA VIRUS;

EID: 1642352884     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1093373     Document Type: Article

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52. I.A.W. is supported by NIH grants CA55896 and AI42266 and National Institute of General Medical Sciences (NIGMS) grant P50-GM 62411. P.P. and C.F.B. are both supported by NIH grants. C.F.B. is an Ellison Medical Foundation New Scholar in Global Infectious Diseases. P.P. is an Ellison Medical Foundation Senior Scholar. J.K.T. is supported by NIH grant AI50619 and by the intramural funds of the Armed Forces Institute of Pathology. This work was carried out in the framework of a multidisciplinary influenza consortium with a pending NIH grant A1058113-01. We thank the staff of the Stanford Synchrotron Radiation Laboratory (SSRL) Beamline 9-2 for the beamline assistance; X. Dai and T. Horton (The Scripps Research Institute) for expert technical assistance; and R. Stanfield, M. Elsliger, and D. Zajonc (The Scripps Research Institute) for helpful discussions. This is publication 16185-MB from The Scripps Research Institute. Coordinates and structure factors have been deposited in the PDB (ID code 1RD8).