1R2A
THE MOLECULAR BASIS FOR PROTEIN KINASE A ANCHORING REVEALED BY SOLUTION NMR
Summary for 1R2A
| Entry DOI | 10.2210/pdb1r2a/pdb |
| NMR Information | BMRB: 4473 |
| Descriptor | PROTEIN (CAMP-DEPENDENT PROTEIN KINASE TYPE II REGULATORY SUBUNIT) (1 entity in total) |
| Functional Keywords | regulatory subunit, anchoring, four-helix bundle, transferase |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 2 |
| Total formula weight | 10796.36 |
| Authors | Newlon, M.G.,Roy, M.,Morikis, D.,Hausken, Z.E.,Coghlan, V.,Scott, J.D.,Jennings, P.A. (deposition date: 1998-12-07, release date: 1998-12-16, Last modification date: 2023-12-27) |
| Primary citation | Newlon, M.G.,Roy, M.,Morikis, D.,Hausken, Z.E.,Coghlan, V.,Scott, J.D.,Jennings, P.A. The molecular basis for protein kinase A anchoring revealed by solution NMR. Nat.Struct.Biol., 6:222-227, 1999 Cited by PubMed Abstract: 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. PubMed: 10074940DOI: 10.1038/6663 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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