By Prof. Dr. Dres. h.c. Harald zur Hausen (auth.)
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Additional resources for Current Cancer Research 1995
It must therefore be observed in an indirect way in order to reconstruct the sequence of events. Just as the protein kinase can recognize the protein to be phosphorylated at a special binding site, so also must this substrate protein display certain structural characteristics in order to be recognized by the enzyme. Proteins should, after a", be phosphorylated specifically, not at random. These recognition sites differ for different protein kinases. In the case of the catalytic subunit of cAMP-dependent protein kinase the substrate is chiefly recognized through two positively charged (so-called basic) amino acid residues lying at a particular distance from the amino acid that will function as phosphoryl receptor.
As well as the possibility of developing a general model of catalysis, the crystal structure of a protein offers further valuable hints and information. The enormous influence protein phosphorylation exerts on cellular processes places the precise control of protein kinase activity at a premium. We have already spoken of the inhibition of protein kinase by fooling it with a pseudosubstrate. Nature has anticipated research in the use of this principle of regulation. Protein kinases are often themselves the substrate for a phosphorylation reaction, for example.
J. BIoI. Chem. 21 Prof. Ingrid Grummt on her morning laboratory round cally, we start working with 300 to 500 liters of cultivated cells. This volume corresponds to approximately 500 billion cells. However, as little as a few millionths of a gram of the RNA-polymerase enzyme and of the transcription factors required for rRNA synthesis are produced. Purification is effected by multiple chromatographs connected in series in which proteins are separated on the basis of different chemical properties, such as charge, size or solubility.