There are currently at least forty-six unique protein kinase crystal structures, twenty-four of
which are available in an active state. Here we examine these structures using a structural …

Protein kinases phosphorylate several cellular proteins providing control mechanisms for
various signalling processes. Their activity is impeded in a number of ways and restored by …

The catalytic activities of eukaryotic protein kinases (EPKs) are regulated by movement of
the C-helix, movement of the N and C lobes upon ATP binding, and movement of the …

About 10% of all protein kinases are predicted to be enzymatically inactive pseudokinases,
but the structural details of kinase inactivation have remained unclear. We present the first …

Amino acid residues associated with functional specificity of cyclin‐dependent kinases
(CDKs), mitogen‐activated protein kinases (MAPKs), glycogen synthase kinases (GSKs) …

Background The widespread protozoan parasite Toxoplasma gondii interferes with host cell
functions by exporting the contents of a unique apical organelle, the rhoptry. Among the mix …

The 2.9 Å crystal structure of the core SRPK1: ASF/SF2 complex reveals that the N-terminal
half of the basic RS domain of ASF/SF2, which is destined to be phosphorylated, is bound to …

A large number of somatic mutations accumulate during the process of tumorigenesis. A
subset of these mutations contribute to tumor progression (known as “driver” mutations) …

The human proteome is rich with protein kinases, and this richness has made the kinase of
crucial importance in initiating and maintaining cell behavior. Elucidating cell signaling …

Phosphotyrosine (pTyr) signaling has evolved into a key cell-to-cell communication system.
Activated receptor tyrosine kinases (RTKs) initiate several pTyr-dependent signaling …