1r2a
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THE MOLECULAR BASIS FOR PROTEIN KINASE A ANCHORING REVEALED BY SOLUTION NMR
OverviewOverview
Compartmentalization of signal transduction enzymes into signaling, complexes is an important mechanism to ensure the specificity of, intracellular events. Formation of these complexes is mediated by, specialized protein motifs that participate in protein-protein, interactions. The adenosine 3',5'-cyclic monophosphate (cAMP)-dependent, protein kinase (PKA) is localized through interaction of the regulatory, (R) subunit dimer with A-kinase-anchoring proteins (AKAPs). We now report, the solution structure of the type II PKA R-subunit fragment, RIIalpha(1-44), which encompasses both the AKAP-binding and dimerization, interfaces. This structure incorporates an X-type four-helix bundle, dimerization motif with an extended hydrophobic face that is necessary for, high-affinity AKAP binding. NMR data on the complex between RIIalpha(1-44), and an AKAP fragment reveals extensive contacts between the two proteins., Interestingly, this same dimerization motif is present in other signaling, molecules, the S100 family. Therefore, the X-type four-helix bundle may, represent a conserved fold for protein-protein interactions in signal, transduction.
About this StructureAbout this Structure
1R2A is a Single protein structure of sequence from Mus musculus. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
ReferenceReference
The molecular basis for protein kinase A anchoring revealed by solution NMR., Newlon MG, Roy M, Morikis D, Hausken ZE, Coghlan V, Scott JD, Jennings PA, Nat Struct Biol. 1999 Mar;6(3):222-7. PMID:10074940
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