de.mpg.escidoc.pubman.appbase.FacesBean
Deutsch
 
Hilfe Wegweiser Impressum Kontakt Einloggen
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT

Freigegeben

Zeitschriftenartikel

The SEP domain of p47 acts as a reversible competitive inhibitor of cathepsin L

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons50556

Sievert,  Volker
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50117

Büssow,  Konrad
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

Externe Ressourcen
Es sind keine Externen Ressourcen verfügbar
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

Soukenik, M., Diehl, A., Leidert, M., Sievert, V., Büssow, K., Leitner, D., et al. (2004). The SEP domain of p47 acts as a reversible competitive inhibitor of cathepsin L. FEBS Letters, 576(3), 358-362. doi:10.1016/j.febslet.2004.09.037.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-8795-9
Zusammenfassung
The solution structure of the human p47 SEP domain in a construct comprising residues G1-S2-p47(171–270) was determined by NMR spectroscopy. A structure-derived hypothesis about the domains' function was formulated and pursued in binding experiments with cysteine proteases. The SEP domain was found to be a reversible competitive inhibitor of cathepsin L with a Ki of 1.5 small mu, GreekM. The binding of G1-S2-p47(171–270) to cathepsin L was mapped by biochemical assays and the binding interface was investigated by NMR chemical shift perturbation experiments.