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

Soukenik, Michael; Diehl, Anne; Leidert, Martina; Sievert, Volker; Büssow, Konrad; Leitner, Dietmar; Labudde, Dirk; Ball, Linda J.; Lechner, Annette; Nägler, Dorit K.; Oschkinat, Hartmut

doi:10.1016/j.febslet.2004.09.037

アイテム詳細

登録内容を編集ファイル形式で保存

一時保存へ追加

タグ情報を表示リリース履歴を表示詳細要約

公開

学術論文

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

MPS-Authors

/persons/resource/persons50556

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

/persons/resource/persons50117

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

External Resource

There are no locators available

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

フルテキスト (公開)

公開されているフルテキストはありません

付随資料 (公開)

There is no public supplementary material available

引用

Soukenik, M., Diehl, A., Leidert, M., Sievert, V., Büssow, K., Leitner, D., Labudde, D., Ball, L. J., Lechner, A., Nägler, D. K., & Oschkinat, H. (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.

引用: https://hdl.handle.net/11858/00-001M-0000-0010-8795-9

要旨

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.