| Autor: |
Soukenik, Michael, Diehl, Anne, Leidert, Martina, Sievert, Volker, Büssow, Konrad, Leitner, Dietmar, Labudde, Dirk, Ball, Linda J., Lechner, Annette, Nägler, Dorit K., Oschkinat, Hartmut |
| Předmět: |
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| Zdroj: |
FEBS Letters; Oct2004, Vol. 576 Issue 3, p358-362, 5p |
| Abstrakt: |
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 μM. 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. [Copyright &y& Elsevier] |
| Databáze: |
Complementary Index |
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