Allosteric regulation of proteases

P. Hauske, C. Ottmann, M. Meltzer, M. Ehrmann, M. Kaiser

Research output: Contribution to journalArticleAcademicpeer-review

63 Citations (Scopus)

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
Original languageEnglish
Pages (from-to)2920-2980
JournalChemBioChem
Volume8
Issue number18
DOIs
Publication statusPublished - 2008

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