1H, 15N and 13C NMR resonance assignments of staphostatin A, a specific Staphylococcus aureus cysteine proteinase inhibitor.
The increasing antibiotic resistance of an important human pathogen Staphylococcus aureus calls for the development of new therapeutic strategies. Staphylococcal cysteine proteases have been suggested as targets for such therapies. The recent discovery of staphostatins, specific protein inhibitors of these enzymes, gives prospects for the design and production of synthetic, low molecular weight analogs which might become drugs. We have decided to structurally characterize staphostatin A, a representative inhibitor of staphylococcal cysteine proteases, and to assess its binding mode to the target protease with the view of clarifying the specificity determinants. Here we report the (1)H, (15)N and (13)C NMR resonance assignments of staphostatin A.
Dubin
Grzegorz
G
Popowicz
Grzegorz
G
Krajewski
Marcin
M
Potempa
Jan
J
Dubin
Adam
A
Holak
Tad A
TA
D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D002247:Carbon Isotopes; D015853:Cysteine Proteinase Inhibitors / Q000737:chemistry*; D006801:Humans; D006859:Hydrogen / Q000737:chemistry; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D011994:Recombinant Proteins / Q000737:chemistry; D013203:Staphylococcal Infections / Q000188:drug therapy; D013211:Staphylococcus aureus / Q000201:enzymology
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D002247:Carbon Isotopes; D015853:Cysteine Proteinase Inhibitors; D009587:Nitrogen Isotopes; D011994:Recombinant Proteins; D006859:Hydrogen