1996年4月19日 · The extracellular α chain is responsible for binding insulin, and the intracellular part of the β chain contains the tyrosine kinase domain, which is flanked by a juxtamembrane region and a C-terminal tail, both of which are targets for phosphorylation. The primary substrate of the insulin receptor is the receptor itself (White and Kahn 1994 ...

Protein phosphorylation is regulated by protein kinases, each of which covalently attaches a phosphate group to an amino acid side chain on serine (Ser), threonine (Thr), or tyrosine (Tyr), and...

Schematic diagram of protein phosphorylation signaling pathway of the extracellular signal‐regulated kinase (ERK), P38, c‐Jun N‐terminal kinase (JNK), apoptosis signal‐regulating kinase (ASK), and Cdc2‐like kinase 2 (CLK2) families in CMGC (cyclin‐dependent kinases, mitogen‐activated protein kinases, glycogen synthase kinases, and ...

2007年8月1日 · Protein kinases have evolved a range of mechanisms to ensure specificity in targeting residues for phosphorylation (see below). One mechanism that ensures specific phosphorylation is the depth...

Protein Phosphorylation plays a critical role in the regulation of cellular function. The cyclin dependent kinases CDK (a serine/threonine kinase family) are responsible for all cell cycle ...

Protein kinases share a common mechanism that is demonstrated in Figure 1, in which the protein function is activated or inactivated by the transfer of a phosphate group from ATP to the free...

Here, we report structural, biochemical, and in vivo data of the responsible kinase, McsB, the founding member of an arginine-specific class of protein kinases. McsB differs in structure and mechanism from protein kinases that act on serine, threonine, and tyrosine residues and instead has a catalytic domain related to phosphagen kinases (PhKs ...

By comparing many protein kinase structures, we are beginning to elucidate general rules of architecture. In addition, I have attempted to illustrate how PKA is regulated by cAMP and how it is localized to specific macromolecular complexes through scaffold proteins.

Background: Activation loop phosphorylation is a conserved mechanism for regulating protein kinases. Results: The unphosphorylated C-subunit structure of protein kinase A shows decoupling of the two lobes of the enzyme. Conclusion: Phosphorylation orients the small and large lobes of the kinase for catalysis.

Serine/threonine protein kinases (EC 2.7.11.1) phosphorylate the OH group of serine or threonine (which have similar side chains). Activity of these protein kinases can be regulated by specific events (e.g., DNA damage), as well as numerous chemical signals, including cAMP / cGMP, diacylglycerol, and Ca 2+ / calmodulin.