Advanced Materials Science Research

Kinome Profiling

 This information is of serious value to our elucidation of the molecular mechanisms that govern cellular physiology. However, an equally, if less , important goal is to define those proteins that participate in signaling pathways that are active in cells. Enzymes that phosphorylate tyrosine, serine and threonine residues on other proteins play a serious role in signaling cascades that determine cell cycle entry, survival, and differentiation fate within the tissues of the body. Most members of the kinase superfamily of enzymes are often recognized from the first sequence by the presence catalytic eukaryotic protein kinase (ePK) domain of roughly 250 amino acids, whereas a way smaller number of protein kinases don't share this catalytic domain and are often collectively called atypical kinases . A comparison of the kinase domains both within and between species displays substantial diversity, which is further complicated by the noncatalytic functional domains of kinases involved in regulation, interactions with other protein partners or the subcellular localisation of kinases. Together, the range in catalytic and noncatalytic domains explains to high degree the functional diversification of kinases within the eukaryotic kingdom.  

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