Crystal structures of the Cid1 poly (U) polymerase reveal the mechanism for UTP selectivity

Nucleic Acids Research

Volumn 40, Issue 19, 2012, Pages 9815-9824

  Lunde, Bradley M ^a   Magler, Iris ^a   Meinhart, Anton ^a  

^a MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; CORDYCEPIN TRIPHOSPHATE; CYTIDINE TRIPHOSPHATE; GUANOSINE TRIPHOSPHATE; HEXOSE 1 PHOSPHATE URIDYLYLTRANSFERASE; HISTIDINE; NUCLEOTIDYLTRANSFERASE; POLY (U) POLYMERASE CID1; UNCLASSIFIED DRUG; URIDINE TRIPHOSPHATE;

ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; KINETOPLASTIDA; MOLECULAR RECOGNITION; MUTATIONAL ANALYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SCHIZOSACCHAROMYCES POMBE;

ADENOSINE TRIPHOSPHATE; CRYSTALLOGRAPHY, X-RAY; CYTIDINE TRIPHOSPHATE; GUANOSINE TRIPHOSPHATE; MODELS, MOLECULAR; MUTATION; NUCLEOTIDYLTRANSFERASES; SCHIZOSACCHAROMYCES POMBE PROTEINS; TRYPANOSOMA BRUCEI BRUCEI; URIDINE TRIPHOSPHATE;

KINETOPLASTIDA;

EID: 84868159990     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks740     Document Type: Article

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