Paper Citing NAMD - Abstract
Cristiani, Andrea; Costa, Giorgio; Cozza, Giorgio; Meggio, Flavio; Scapozza, Leonardo; Moro, Stefano
The Role of the N-Terminal Domain in the Regulation of the "Constitutively Active" Conformation of Protein Kinase CK2 alpha: Insight from a Molecular Dynamics Investigation
CHEMMEDCHEM, 6:1207-1216, JUL 4 2011
Protein kinase CK2 is an extremely well-conserved pleiotropic protein kinase with a growing list of substrates, the majority of which are proteins implicated in signal transduction, gene expression, and transcription-related functions. Protein kinase CK2 is a ubiquitous heterotetrameric serine/threonine protein kinase made up of two a or alpha' catalytic subunits and two beta regulatory subunits. Moreover, protein kinase CK2 is defined as a "constitutively active" protein kinase in contrast to most other protein kinases characterized by the presence of distinct conformations associated with the active and inactive states. As previously demonstrated by in vitro mutation studies, CK2 activity is substantially regulated by the interaction between the N-terminal tail and the kinase domain. In fact, progressive deletions of the N-terminal tail show a decrease in the activity
