吩噻嗪
变构调节
化学
立体化学
计算生物学
计算机科学
药理学
生物化学
医学
生物
酶
作者
Florian Schlauderer,Katja Lammens,Daniel Nagel,Michelle Vincendeau,Andrea C. Eitelhuber,Steven H. L. Verhelst,Dale Kling,A Chruściel,Jürgen Ruland,Daniel Krappmann,Karl‐Peter Hopfner
标识
DOI:10.1002/anie.201304290
摘要
Second site: In the crystal structure of human MALT1casp-Ig3 (mucosa-associated lymphoid tissue lymphoma translocation protein 1) in complex with the tricyclic phenothiazine derivative thioridazine (violet in the picture), the inhibitor is bound in a hydrophobic pocket far from the active site. This explains the action of phenothiazine derivatives as noncompetitive, reversible inhibitors.
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