Hauske, Patrick; Otmann, Christian; Meltzer, Michael; Ehrmann, Michael; Kaiser, Markus:
Allosteric regulation of proteases.
In: ChemBioChem : a European journal of chemical biology, Jg. 9 (2008), Heft 18, S. 2920 - 2928
2008Artikel/Aufsatz in Zeitschrift
BiologieFakultät für Biologie
Allosteric regulation of proteases.
Hauske, PatrickLSF; Otmann, Christian; Meltzer, MichaelLSF; Ehrmann, MichaelLSF; Kaiser, Markus


Allostery is a basic principle of control of enzymatic activities based on the interaction of a protein or small molecule at a site distinct from an enzyme's active center. Allosteric modulators represent an alternative approach to the design and synthesis of small-molecule activators or inhibitors of proteases and are therefore of wide interest for medicinal chemistry. The structural bases of some proteinaceous and small-molecule allosteric protease regulators have already been elucidated, indicating a general mechanism that might be exploitable for future rational design of small-molecule effectors.