Protein kinases domain

Other less well-characterized effectors of Ras proteins are the proteins Rinl and AF6 (review Vojtek and Der, 1998) and the product of the ksr gene. The KSR protein (KSR = kinase suppressor of Ras) has a protein kinase domain which is 31 % identical to the kinase domain of Raf kinase (review Downward, 1995). It is not clear how KSR kinase participates in Ras signal transduction. 

Bernards A. Predicted tyk2 protein contains two tandem protein kinase domains. Oncogene 1991 6 1185-1187. 

The binding of a hormone or growth factor (a ligand) to a dimeric receptor activates the protein kinase domain of the receptor which phosphorylates a number of tyrosine hydroxyl groups of the receptor itself. This autophosphorylation is followed by a variety of events, which include phosphorylation of tyrosine side chains of various other proteins.426 An-... 

Under the electron microscope titin appears as a flexible beaded string 4 nm in diameter. Most of the molecule is made up of repetitive domains of two types. In human cardiac titin there are 132 folded domains that resemble type III fibronectin repeats and 112 immunoglobulin-like domains.98 In a "PEVK region," between residues 163 and 2174, 70% of the residues are Pro, Glu, Val, or Lys. The titin molecule may be organized as polyproline helices in this elastic region.1023 At the C terminus of titin 800 residues, including a Ser / Thr protein kinase domain, are found within the M-line. 

Harmar AJ (2001) Family-B G-protein-coupled receptors. Genome Biol 2 3013.1-3013.10 Hata Y, Butz S, Stidhof TC (1996) CASK a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins. J Neurosci 16 2488-94... 

PINKl is located on chromosome lp36.12 and has eight exons and cDNA that spans 1.8 kb. It encodes a protein with 581 amino acids. It has a serine/threonine protein kinase domain. However, its function is not known (Valente et al., 2001). It is a mitochondrial protein located in the matrix and the intermembrane space that is ubiquitously expressed in the brain and systemic organs and contains a mitochondrial-targeting motif and a conserved serine/threonine kinase domain (Silvestri et al., 2005). 

E. coli Histidine protein kinase domain lAOB 11 Glrw 3 Glrw 25 His (N) Aspa ... 

Tyrosine domain and an intracellular protein kinase domain. Receptor tyrosine kinases... 

Figure 15.26. Janus Kiuase Domaiu Structure. A Janus kinase (JAK) includes four recognized domains an ERM domain that favors interactions with membranes, an SH2 domain that binds phosphotyrosine-containing peptides, and two domains homologous to protein kinases. Only the second protein kinase domain appears to be enzymatically functional.

Figure 15.35. Sre Structure. (A) Cellular Sre includes an SH3 domain, an SH2 domain, a protein kinase domain, and a carboxyl-terminal tail that includes a key tyrosine residue. (B) Structure of c-Src in an inactivated form with the key tyrosine residue phosphorylated. The phosphotyrosine residue is bound in the SH2 domain the linker between the SH2 domain and the protein kinase domain is bound by the SH3 domain. These interactions hold the kinase domain in an inactive conformation.

Other proteins crucial to signal-transduction pathways arose much later. For example, the eukaryotic protein kinases are one of the largest protein families in all eukaryotes and yet appear to be absent in prokaryotes. The evolution of the eukaryotic protein kinase domain appears to have been an important biochemical step in the appearance of eukaryotes and the subsequent development of multicellular organisms. 

Each p subunit consists primarily of a protein kinase domain, homologous to protein kinase A. This kinase differs from protein kinase A in two important ways. First, the insulin receptor kinase is a tyrosine kinase that is, it catalyzes the transfer of a phosphoryl group from ATP to the hydroxyl group of tyrosine, rather than serine or threonine, as is the case for protein kinase A. 

Figure 14.19 Activation of the insulin receptor by phosphorylation. The activation loop is shown in red in this model of the protein kinase domain of the fi subunit of The Insulin receptor. The unphosphorylated structure on the left is not catalytically active. Notice that, when three tyrosine residues in the activation loop are phosphorylated, the activation loop swings across the structure and the kinase structure adopts a more compact conformation. This conformation is catalytically active. [Drawn from lIRK.pdb and IR3.pdb.]...

Cyclic AMP-dependent N fnlracailular protein kinases ) domain... 

Although there is no similarity to classical protein kinases on the primary sequence level, the three-dimensional structure of the TRP channel protein kinase domain is very similar to the classical kinase fold. 

Multifunctional Ca2+/calmodulin-dependent protein kinase Domain structure and regulation, H. Schulman and L. 

---