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ID: 230810.0, MPI für molekulare Genetik / Department of Vertebrate Genomics
The SEP domain of p47 acts as a reversible competitive inhibitor of cathepsin L
Authors:Soukenik, Michael; Diehl, Anne; Leidert, Martina; Sievert, Volker; Büssow, Konrad; Leitner, Dietmar; Labudde, Dirk; Ball, Linda J.; Lechner, Annette; Nägler, Dorit K.; Oschkinat, Hartmut
Language:English
Date of Publication (YYYY-MM-DD):2004-10-22
Title of Journal:FEBS Letters
Journal Abbrev.:FEBS Lett
Volume:576
Issue / Number:3
Start Page:358
End Page:362
Copyright:© 2004 Federation of European Biochemical Societies. Published by Elsevier B.V.
Review Status:not specified
Audience:Experts Only
Abstract / Description: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.
Free Keywords:SEP; p97; p47; Cathepsin L; NMR; Protein structure
Comment of the Author/Creator:Published online: 2004-09-25
External Publication Status:published
Document Type:Article
Communicated by:Hans Lehrach
Affiliations:MPI für molekulare Genetik
External Affiliations:Forschungsinstitut für Molekulare Pharmakologie, Robert-Rössle Str. 10, D-13125 Berlin, Germany;
Proteinstrukturfabrik, Berlin, Germany;
Freie Universitaet Berlin, Berlin, Germany;
Department of Clinical Chemistry and Clinical Biochemistry, LMU Munich, Germany
Identifiers:ISSN:0014-5793
DOI:10.1016/j.febslet.2004.09.037
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