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      Mechanisms of specificity in protein phosphorylation.

      Nature reviews. Molecular cell biology

      Substrate Specificity, Static Electricity, Protein Structure, Tertiary, Protein Structure, Secondary, metabolism, classification, chemistry, Protein Kinases, Protein Binding, Phosphorylation, NIH 3T3 Cells, Models, Molecular, Models, Biological, Mice, Hydrophobic and Hydrophilic Interactions, Humans, Forecasting, Consensus Sequence, Binding Sites, Animals, Amino Acid Sequence, Amino Acid Motifs, Adenosine Triphosphate, Adenosine Diphosphate

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          Abstract

          A typical protein kinase must recognize between one and a few hundred bona fide phosphorylation sites in a background of approximately 700,000 potentially phosphorylatable residues. Multiple mechanisms have evolved that contribute to this exquisite specificity, including the structure of the catalytic site, local and distal interactions between the kinase and substrate, the formation of complexes with scaffolding and adaptor proteins that spatially regulate the kinase, systems-level competition between substrates, and error-correction mechanisms. The responsibility for the recognition of substrates by protein kinases appears to be distributed among a large number of independent, imperfect specificity mechanisms.

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          Journal
          17585314
          10.1038/nrm2203

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