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

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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;

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Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-8795-9
Abstract
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.