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Inside Cover: Insights into Matriptase‐2 Substrate Binding and Inhibition Mechanisms by Analyzing Active‐Site‐Mutated Variants (ChemMedChem 1/2012)
Author(s) -
Maurer Eva,
Sisay Mihiret T.,
Stirnberg Marit,
Steinmetzer Torsten,
Bajorath Jürgen,
Gütschow Michael
Publication year - 2012
Publication title -
chemmedchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201190061
Subject(s) - active site , chemistry , cover (algebra) , substrate (aquarium) , binding site , protease , computational biology , mutation , serine protease , stereochemistry , biochemistry , combinatorial chemistry , catalysis , biology , enzyme , gene , engineering , mechanical engineering , ecology
The inside cover picture shows a homology model of the catalytic domain of matriptase‐2, a protease that plays a key role in human iron homeostasis. A substrate‐analogue inhibitor was docked into the active site of a mutated variant of matriptase‐2. A detailed view of the complex is presented on the right. The mutation is highlighted in green. For more details, please see the Communication by Michael Gütschow et al. on p. 68 ff.