The large groove found in the gH/gL structure is an important functional domain for epstein-barr virus fusion

Journal of Virology

Volumn 87, Issue 7, 2013, Pages 3620-3627

  Chen, Jia ^a   Jardetzky, Theodore S ^b   Longneckera, Richard ^a  

^a NORTHWESTERN UNIVERSITY   (United States)

^b STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINO ACID; CYSTEINE; DITHIOTHREITOL; GLYCINE; GLYCOPROTEIN L; HISTIDINE; LEUCINE; PROLINE; PROTEIN GH; PROTEIN GP42; THREONINE; UNCLASSIFIED DRUG; VALINE; VIRUS GLYCOPROTEIN; VIRUS PROTEIN;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; B LYMPHOCYTE; CELL ACTIVITY; CELL FUSION; CONTROLLED STUDY; DISULFIDE BOND; EMBRYO; EPITHELIUM CELL; EPSTEIN BARR VIRUS; GENE CONSTRUCT; GENE REARRANGEMENT; HUMAN; HUMAN CELL; MEMBRANE FUSION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS;

ANIMALS; BLOTTING, WESTERN; CHO CELLS; CRICETINAE; CRICETULUS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME-LINKED IMMUNOSORBENT ASSAY; HERPESVIRUS 4, HUMAN; LUCIFERASES; MEMBRANE GLYCOPROTEINS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MULTIPROTEIN COMPLEXES; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN CONFORMATION; VIRAL PROTEINS; VIRUS INTERNALIZATION;

HUMAN HERPESVIRUS 4;

EID: 84875527382     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.03245-12     Document Type: Article

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