Structural Characteristics of Protein Kinases and Their Inhibitors in Clinical Use

Abstract

Protein kinases (PKs) are enzymes responsible for transferring the γ-phosphate group from adenosine triphosphate (ATP) to target proteins, mediating a wide range of signal transduction pathways and regulating different cellular activities. The deregulation and/or overexpression of these protein kinases result in inappropriate cellular responses, culminating in the establishment and development of several diseases, e.g. diabetes, inflammatory diseases and cancer. Since PKs account for around 22 % of the proteins encoded by the human druggable genome, they have been widely recognized as promising therapeutic targets for treatment of different diseases. This review details the main structural features of protein kinases, as well as their physiological functions and inhibitors in clinical use.

The p38 MAPK Inhibitors and Their Role in Inflammatory Diseases

“…Protein kinases (PKs) are enzymes that transfer the adenosine triphosphate γ-phosphate group (ATP) to target proteins. [1] The mitogen-activated protein kinase (MAPK) is a family of protein kinases that are evolutionally conserved and have evolved to transduce environmental and developmental signals into adaptive and programmed responses such as differentiation, inflammation, and apoptosis. [2] The MAPK family consists of three major members: extracellular signal regulated kinases (ERK), p38 and c-Jun N-terminal kinase (JNK), which represents three different signaling cascades.…”