Structure of thymidylate kinase reveals the cause behind the limiting step in AZT activation

Nature Structural Biology

Volumn 4, Issue 8, 1997, Pages 601-604

  Lavie, A ^a   Vetter, I R ^a   Konrad, M ^a   Goody, R S ^a   Reinstein, J ^a   Schlichting, I ^a  

^a MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOTRANSFERASE; THYMIDINE PHOSPHATE; ZIDOVUDINE; ZIDOVUDINE 5' PHOSPHATE;

ARTICLE; DRUG ACTIVATION; DRUG DEVELOPMENT; ENZYME BINDING; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; NONHUMAN; PRIORITY JOURNAL;

COMPUTER SIMULATION; CRYSTALLOGRAPHY; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; MOTION; NUCLEOSIDE-PHOSPHATE KINASE; PHOSPHORYLATION; PRODRUGS; SACCHAROMYCES CEREVISIAE; SUBSTRATE SPECIFICITY; THYMIDINE MONOPHOSPHATE; THYMINE NUCLEOTIDES; ZIDOVUDINE;

EID: 0030845913     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0897-601     Document Type: Article

References (28)