| Staphylokinase is a bacterial plasminogen activator protein which is currently in clinical
testing for treatment of myocardial infarction and peripheral thrombosis.
We have recently completed a structural determination of the wild type
protein and are currently investigating structural and functional properties
of a series of staphylokinase mutants with a view to engineering this protein
to improve clinical properties. (The figure was prepared using the program MOLMOL (Koradi et al., 1996)) |
Related publications:
O. Ohlenschläger, R. Ramachandran, K. Gührs, B. Schlott and L. R. Brown.
"Structural investigations on the activation of plasminogen by staphylokinase"
Bulletin of Magnetic Resonance 20(1/4) (1999), 35-38.
O. Ohlenschläger, R. Ramachandran, K. Gührs, B. Schlott and L. R. Brown.
"Nuclear magnetic resonance solution structure of the plasminogen-activator protein staphylokinase"
Biochemistry 37 (1998), 10635-10642.
[Abstract]
[PDB code: 1SSN]
O. Ohlenschläger, R. Ramachandran, J. Flemming, K. Gührs,
B. Schlott and L. R. Brown.
"NMR secondary structure of the plasminogen activator protein staphylokinase"
Journal of Biomolecular NMR 9 (1997), 273-286.
[Abstract]