NMR structure of an inhibitory R2 C-terminal peptide bound to mouse ribonucleotide reductase R1 subunit.
The structure of peptide N-AcYTLDADF when bound to the large subunit of mouse ribonucleotide reductase has been elucidated by transfer NOE. This structure suggests a general design for type 1 RR inhibitors.
Fisher
A
A
Laub
P B
PB
Cooperman
B S
BS
D000595:Amino Acid Sequence; D000818:Animals; D015195:Drug Design; D009682:Magnetic Resonance Spectroscopy; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D012264:Ribonucleotide Reductases / Q000037:antagonists & inhibitors* / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
C096714:N-acetyltyrosyl-threonyl-leucyl-aspartyl-alanyl-aspartyl-phenylalanine; D009842:Oligopeptides; D012264:Ribonucleotide Reductases