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) ; Nr. 18, S. 2920-2928
ISSN: 1439-4227
Zeitschriftenaufsatz / Fach: Biologie
ehem. Fakultät für Biologie und Geografie
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.