Crystallographic and biochemical analysis of rotavirus NSP2 with nucleotides reveals a nucleoside diphosphate kinase-like activity.

Kumar, Mukesh; Jayaram, Hariharan; Vasquez-Del Carpio, Rodrigo; Jiang, Xiaofang; Taraporewala, Zenobia F; Jacobson, Raymond H; Patton, John T; Prasad, B V Venkataram

Kumar, Mukesh; Jayaram, Hariharan; Vasquez-Del Carpio, Rodrigo; Jiang, Xiaofang; Taraporewala, Zenobia F; Jacobson, Raymond H; Patton, John T; Prasad, B V Venkataram.

Affiliation

Kumar M; Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.

J Virol ; 81(22): 12272-84, 2007 Nov.

Article in En | MEDLINE | ID: mdl-17804496

Subject(s)

Nucleoside-Diphosphate Kinase/chemistry; Nucleotides/chemistry; RNA-Binding Proteins/chemistry; Viral Nonstructural Proteins/chemistry; Adenosine Triphosphate/analogs & derivatives; Adenosine Triphosphate/chemistry; Amino Acid Sequence; Animals; Binding Sites; Catalysis; Catalytic Domain; Humans; Kinetics; Molecular Sequence Data; Nucleoside-Diphosphate Kinase/genetics; Nucleoside-Diphosphate Kinase/physiology; Phosphorylation; Protein Conformation; RNA-Binding Proteins/genetics; RNA-Binding Proteins/physiology; Rotavirus/enzymology; Rotavirus/physiology; Viral Nonstructural Proteins/genetics; Viral Nonstructural Proteins/physiology; Virus Replication

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: RNA-Binding Proteins / Viral Nonstructural Proteins / Nucleoside-Diphosphate Kinase / Nucleotides Limits: Animals / Humans Language: En Journal: J Virol Year: 2007 Document type: Article Affiliation country: United States

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