Allosteric Regulation of Proteases |
| |
Authors: | Patrick Hauske Christian Ottmann Dr Michael Meltzer Michael Ehrmann Prof Dr Markus Kaiser Dr |
| |
Affiliation: | 1. Chemical Genomics Centre der Max‐Planck‐Gesellschaft, Otto‐Hahn‐Strasse 15, 44227 Dortmund (Germany), Fax: (+49)?231‐9742‐6479;2. Zentrum für Medizinische Biotechnologie, FB Biologie und Geographie, Universit?t Duisburg‐Essen, 45117 Essen (Germany) |
| |
Abstract: | 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. |
| |
Keywords: | allosteric regulation drug discovery enzymes proteases small molecules |
|