Structure of thymidylate kinase reveals the cause behind the limiting step in AZT activation.
Lavie
A
A
Vetter
I R
IR
Konrad
M
M
Goody
R S
RS
Reinstein
J
J
Schlichting
I
I
D003198:Computer Simulation; D003461:Crystallography; D054306:Dideoxynucleotides; D008958:Models, Molecular; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D009038:Motion; D009703:Nucleoside-Phosphate Kinase / Q000737:chemistry* / Q000378:metabolism; D010766:Phosphorylation; D011355:Prodrugs / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013379:Substrate Specificity; D013938:Thymidine Monophosphate / Q000737:chemistry* / Q000378:metabolism; D013942:Thymine Nucleotides / Q000737:chemistry* / Q000378:metabolism; D015215:Zidovudine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism*
D054306:Dideoxynucleotides; D011355:Prodrugs; D013942:Thymine Nucleotides; C057287:3'-azido-3'-deoxythymidine 5'phosphate; D013938:Thymidine Monophosphate; D015215:Zidovudine; D009703:Nucleoside-Phosphate Kinase; C020093:dTMP kinase