Journal article
Crystal structures of the catalytic subunit of cAMP-dependent protein kinase reveal general features of the protein kinase family
Publication Details
Authors: | Taylor, S.; Radzio-Andzelm, E.; Knighton, D.; Eyck, L.; Sowadski, J.; Herberg, F.; Yonemoto, W.; Zheng, J. |
Publication year: | 1993 |
Journal: | Receptor |
Pages range : | 165–172 |
Volume number: | 3 |
ISSN: | 2813-2564 |
eISSN: | 2813-2564 |
URN / URL: |
Abstract
The crystal structure of the catalytic subunit of cAMP-dependent protein kinase serves as a template for the catalytic core of all eukaryotic protein kinases. The various crystal structures are reviewed with particular emphasis on the numerous conserved residues that converge at the active site. The structures also reveal the importance of posttranslational modifications, including myristylation and phosphorylation.
The crystal structure of the catalytic subunit of cAMP-dependent protein kinase serves as a template for the catalytic core of all eukaryotic protein kinases. The various crystal structures are reviewed with particular emphasis on the numerous conserved residues that converge at the active site. The structures also reveal the importance of posttranslational modifications, including myristylation and phosphorylation.
Keywords
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