How mitogen-activated protein kinases recognize and phosphorylate their targets: A QM/MM study.

ABSTRACT: Mitogen-activated protein kinase (MAPK) signaling pathways play an essential role in the transduction of environmental stimuli to the nucleus, thereby regulating a variety of cellular processes, including cell proliferation, differentiation, and programmed cell death. The components of the MAPK extracellular activated protein kinase (ERK) cascade represent attractive targets for cancer therapy, as their aberrant activation is a frequent event among highly prevalent human cancers. To understand how MAPKs recognize and phosphorylate their targets is key to unravel their function. However, these events are still poorly understood because of the lack of complex structures of MAPKs with their bound targets in the active site. Here we have modeled the interaction of ERK with a target peptide and

SUBMITTER: Turjanski AG 

PROVIDER: S-EPMC2754815 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature