2. Academic Validation
  3. The SEP domain of p47 acts as a reversible competitive inhibitor of cathepsin L

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

  • FEBS Lett. 2004 Oct 22;576(3):358-62. doi: 10.1016/j.febslet.2004.09.037.
Michael Soukenik 1,  Anne Diehl,  Martina Leidert,  Volker Sievert,  Konrad Büssow,  Dietmar Leitner,  Dirk Labudde,  Linda J Ball,  Annette Lechner,  Dorit K Nägler,  Hartmut Oschkinat
Affiliations

Affiliation

  • 1 Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle Str. 10, D-13125 Berlin, Germany.
PMID: 15498563 DOI: 10.1016/j.febslet.2004.09.037
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 microM. 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.

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