Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR

Science

Volumn 286, Issue 5444, 1999, Pages 1579-1583

  Bewley, Maria C ^a   Springer, Karen ^a   Zhang, Yian Biao ^a   Freimuth, Paul ^a   Flanagan, John M ^a  

^a BROOKHAVEN NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL RECEPTOR; VIRUS RECEPTOR;

ADENOVIRUS; ADENOVIRUS 12; ARTICLE; BINDING SITE; CLONING VECTOR; COXSACKIE VIRUS; CRYSTAL STRUCTURE; GENE THERAPY; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; RECEPTOR BINDING; VIRUS INFECTION;

ADENOVIRUSES, HUMAN; AMINO ACID SUBSTITUTION; BINDING SITES; CAPSID; CAPSID PROTEINS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; MODELS, MOLECULAR; MUTAGENESIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECEPTORS, VIRUS; RECOMBINANT PROTEINS; THERMODYNAMICS;

ADENOVIRIDAE; COXSACKIEVIRUS; DNA VIRUSES; HUMAN ADENOVIRUS TYPE 12;

EID: 0033584785     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.286.5444.1579     Document Type: Article

References (32)

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32. The authors thank V. Graziano for analyzing the binding affinities of the knob variants; M. Rossmann, D. Engelman, C. Anderson, J. Dunn, and J. Kuryian for critically reading the manuscript and suggesting improvements; and L. Berman, R. Sweet, and J. Berendsen for access to beamlines X25, X12C, and X8C, respectively. This research was supported by NIH grant AI362S1 to P.F. and by the Office of Biological and Environmental Research of the U.S. Department of Energy under Prime Contract DE-AC02-98CH10886 with Brookhaven National Laboratory. The macromolecular crystallography beamlines X25, X12C, and X8C, at the National Synchrotron Light Source, are also supported by NSF and by NIH grant 1P41 RR12408-01A1. Coordinates have been deposited in the Protein Data Bank with accession codes 1NOB and 1KAC for Ad12 knob and Ad12 knob in complex with CAR D1, respectively.