Letter to the Editor: 1H, 15N and 13C NMR Resonance Assignments of Staphostatin A, a Specific Staphylococcus Aureus Cysteine Proteinase Inhibitor
Source: Journal of Biomolecular NMR, Volume 28, Number 3, March 2004 , pp. 295-296(2)
Abstract: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 1H, 15N and 13C NMR resonance assignments of staphostatin A.
Document Type: Research article
Affiliations: 1: Faculty of Biotechnology, Jagiellonian University, ul. Gronostajowa 7, 30-387 Krakow, Poland, Email: firstname.lastname@example.org 2: Max-Planck-Institute for Biochemistry, Am Klopferspitz 18A, D-82152 Martinsried, Germany 3: Faculty of Biotechnology, Jagiellonian University, ul. Gronostajowa 7, 30-387 Krakow, Poland
Publication date: 2004-03-01