Comparison of the solution structures of microcystin-LR and motuporin.
A comparison of the structures of two cyanobacterial toxins yields insights into how they may inhibit protein phosphatase-1 and -2A and why microcystins but not motuporin may covalently modify their protein phosphatase targets.
Bagu
J R
JR
Sönnichsen
F D
FD
Williams
D
D
Andersen
R J
RJ
Sykes
B D
BD
Holmes
C F
CF
D000595:Amino Acid Sequence; D009682:Magnetic Resonance Spectroscopy; D008387:Marine Toxins; D052998:Microcystins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010456:Peptides, Cyclic / Q000737:chemistry* / Q000494:pharmacology; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors*; D011485:Protein Binding; D054645:Protein Phosphatase 1; D017434:Protein Structure, Tertiary; D012996:Solutions
D008387:Marine Toxins; D052998:Microcystins; D010456:Peptides, Cyclic; D012996:Solutions; C093605:motuporin; C063998:nodularin; C093607:microcystin LL; C049865:cyanoginosin-LA; D010749:Phosphoprotein Phosphatases; D054645:Protein Phosphatase 1; C057862:cyanoginosin LR