Strukturelle Analyse Von Phenothiazin‐Derivaten Als Allosterische Inhibitoren Der MALT1‐Paracaspase

Die Kristallstruktur von humanem MALT1 (mucosa-associated lymphoid tissue lymphoma translocation protein 1), bestehend aus der Paracaspase und der C-terminalen Ig3-Domäne, in Komplex mit dem tricyclischen Phenothiazin-Derivat Thioridazin (violett im Bild) zeigt den Inhibitor an einer weit vom aktiven Zentrum entfernten Bindungsstelle. Dies erklärt warum Phenothiazin-Derivate als nichtkompetitive, reversible Inhibitoren wirken. As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.