The crystal structure of the Epstein-Barr virus protease shows rearrangement of the processed C terminus

Journal of Molecular Biology

Volumn 324, Issue 1, 2002, Pages 89-103

  Buisson, Marlyse ^a,b,c   Hernandez, Jean François ^d,e   Lascoux, David ^e   Schoehn, Guy ^b,e   Forest, Eric ^e   Arlaud, Gérard ^e   Seigneurin, Jean Marie ^a,c   Ruigrok, Rob W H ^b,c   Burmeister, Wim P ^b,c  

^a HÔPITAL MICHALLON   (France)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (France)

^c UNIV GRENOBLE ALPES   (France)

^d UNIVERSITÉ DE MONTPELLIER   (France)

^e INSTITUT DE BIOLOGIE STRUCTURALE   (France)

Author keywords

Crystal structure; Enzymatic activity; Herpesvirus; Protease; Virus assembly

Indexed keywords

ASSEMBLIN; DYFLOS; PROTEINASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; CYTOMEGALOVIRUS; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME INHIBITION; ENZYME STRUCTURE; EPSTEIN BARR VIRUS; ESCHERICHIA COLI; PRIORITY JOURNAL; PROTEIN EXPRESSION; SEQUENCE ALIGNMENT; X RAY CRYSTALLOGRAPHY;

CYTOMEGALOVIRUS; ESCHERICHIA COLI; HERPESVIRIDAE; HUMAN HERPESVIRUS 4; HUMAN HERPESVIRUS 8;

EID: 0036435906     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01040-9     Document Type: Article

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