LMP1 protein from the Epstein-Barr virus is a structural CD40 decoy in B lymphocytes for binding to TRAF3

Journal of Biological Chemistry

Volumn 280, Issue 39, 2005, Pages 33620-33626

  Wu, ShuangDing ^a   Xie, Ping ^b   Welsh, Kate ^a   Li, Chenglong ^a,c   Ni, Chao Zhou ^a   Zhu, Xiuwen ^a,c   Reed, John C ^a   Satterthwait, Arnold C ^a   Bishop, Gail A ^b   Ely, Kathryn R ^a  

^a BURNHAM INSTITUTE   (United States)

^b UNIVERSITY OF IOWA   (United States)

^c SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; CRYSTAL STRUCTURE; HYDROGEN BONDS; VIRUSES;

B LYMPHOCYTES; EPSTEIN-BARR VIRUS; LMP1 PROTEIN; MONONUCLEOSIS;

PROTEINS;

ARGININE; ASPARTIC ACID; CD40 ANTIGEN; LATENT MEMBRANE PROTEIN 1; MEMBRANE PROTEIN; TUMOR NECROSIS FACTOR DERIVATIVE; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 1; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 3; TYROSINE; UNCLASSIFIED DRUG; VIRUS PROTEIN;

ANIMAL CELL; ARTICLE; B LYMPHOCYTE; B LYMPHOCYTE ACTIVATION; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONTROLLED STUDY; CYTOPLASM; EPSTEIN BARR VIRUS; HERPES SIMPLEX VIRUS; HYDROGEN BOND; INFECTIOUS MONONUCLEOSIS; LYMPHOCYTE TRANSFORMATION; LYMPHOPROLIFERATIVE DISEASE; MOLECULAR RECOGNITION; MOLECULAR STABILITY; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; SIGNAL TRANSDUCTION;

ALANINE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; ANTIGENS, CD40; B-LYMPHOCYTES; BINDING SITES; BLOTTING, WESTERN; CELL TRANSFORMATION, VIRAL; CRYSTALLOGRAPHY, X-RAY; HERPESVIRUS 4, HUMAN; HUMANS; LYMPHOCYTE ACTIVATION; MICE; MICROSCOPY, FLUORESCENCE; MODELS, MOLECULAR; PRECIPITIN TESTS; TNF RECEPTOR-ASSOCIATED FACTOR 3; TRANSFECTION; VIRAL MATRIX PROTEINS;

ANIMALIA; HERPESVIRIDAE; HUMAN HERPESVIRUS 4; SIMPLEXVIRUS;

EID: 25844450231     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M502511200     Document Type: Article

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