1999
DOI: 10.1016/s0079-6107(98)00059-5
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The catalytic subunit of cAMP-dependent protein kinase: prototype for an extended network of communication

Abstract: The protein kinase catalytic core in essence comprises an extended network of interactions that link distal parts of the molecule to the active site where they facilitate phosphoryl transfer from ATP to protein substrate. This review defines key sequence and structural elements, describes what is currently known about the molecular interactions, and how they are involved in catalysis.

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Cited by 100 publications
(91 citation statements)
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“…2d). Arg-56 is next to Phe-54 and Gly-55, the two ATP-binding residues in PKA (12). We first analyze the PSDRs near or in contact with the substrate, using the well known PKA-inhibitor-complex structure from ref.…”
Section: Resultsmentioning
confidence: 99%
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“…2d). Arg-56 is next to Phe-54 and Gly-55, the two ATP-binding residues in PKA (12). We first analyze the PSDRs near or in contact with the substrate, using the well known PKA-inhibitor-complex structure from ref.…”
Section: Resultsmentioning
confidence: 99%
“…'' In eukaryotes, PKs are classified into eight main groups (2,11). Most of them are involved in signal transduction (12)(13)(14). In this paper, we focus on the cAMP-dependent PK, cGMP- dependent PK, and PKC (AGC) group of Ser͞Thr PKs.…”
mentioning
confidence: 99%
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“…60 All protein kinases share a significant degree of sequence and structural conservation throughout the ~250 amino acid catalytic core of these enzymes. [67][68][69][70] This arginine residue is one of a few positions in the kinase domain that is absolutely conserved throughout the protein kinase family. 60 Therefore, it will be important to test whether alterations at this position in other protein kinases will lead to a similar increase in substrate binding.…”
Section: Kinase Substrate Trap Assaymentioning
confidence: 99%