Crystal structure of the papain-like protease of MERS coronavirus reveals unusual, potentially druggable active-site features

Antiviral Research

Volumn 109, Issue 1, 2014, Pages 72-82

  Lei, Jian ^a,c   Mesters, Jeroen R ^a,c   Drosten, Christian ^b,c   Anemüller, Stefan ^a,c   Ma, Qingjun ^a,c   Hilgenfeld, Rolf ^a,c  

^a UNIVERSITY OF LÜBECK   (Germany)

^b UNIVERSITY OF BONN   (Germany)

^c German Center for Infection Research (DZIF) Germany German Center for Infection Research (DZIF)   (Germany)

Author keywords

Antiviral drug design; Deubiquitinase; MERS CoV; Oxyanion hole; Papain like protease; Zinc finger

Indexed keywords

PAPAIN; UBIQUITIN; VIRUS PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONFORMATIONAL TRANSITION; CORONAVIRUS; CRYSTAL STRUCTURE; CRYSTALLIZATION; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; HYDROLYSIS; IN VITRO STUDY; MIDDLE EAST RESPIRATORY SYNDROME CORONAVIRUS; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; SARS CORONAVIRUS; THREE DIMENSIONAL IMAGING; X RAY CRYSTALLOGRAPHY; AMINO ACID SEQUENCE; ANTAGONISTS AND INHIBITORS; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GENETICS; MOLECULAR GENETICS; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; MIDDLE EAST RESPIRATORY SYNDROME CORONAVIRUS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PAPAIN; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; VIRAL PROTEINS;

EID: 84904345425     PISSN: 01663542     EISSN: 18729096     Source Type: Journal    
DOI: 10.1016/j.antiviral.2014.06.011     Document Type: Article

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