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| home > ebr > winter 2003 > understanding drug-kinase interactions with surface plasmon resonance (spr) |
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European Biopharmaceutical Review
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| Protein kinases (PKs) represent one of the largest known superfamilies of human proteins. A recent report identified 510 candidate PK genes on the basis of sequence homology (1). PKs play critical roles in almost all signal transduction pathways, such as post-receptor cascades (2). Upstream signalling events are relayed by the action of PKs, usually via their phosphorylation of key serine, threonine or tyrosine residues on target proteins, using ATP or GTP as phosphate donors (3). These functions are carried out by a 250 amino acid catalytic domain, which is conserved among and used to identify members of the PK superfamily (4). This domain consists of an N-terminal lobe that binds and orientates the ATP/GTP, and a larger C-terminal lobe, which binds to the target protein and catalyses the transfer of phosphate. |
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