2H9R

Docking and dimerization domain (D/D) of the regulatory subunit of the Type II-alpha cAMP-dependent protein kinase A associated with a Peptide derived from an A-kinase anchoring protein (AKAP)

Summary for 2H9R

• Entry DOI: 10.2210/pdb2h9r/pdb
• Related: 1L6E 1R2A 2DRN 2HWN
• Descriptor: cAMP-dependent protein kinase type II-alpha regulatory subunit, 22-mer from A-kinase anchor protein 5 (2 entities in total)
• Functional Keywords: akap, pka, signal transduction, 4-helix bundle, helix-loop-helix, protein-peptide complex, transferase
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Membrane: P24588
• Total number of polymer chains: 3
• Total formula weight: 13180.16

Authors

Newlon, M.G.,Roy, M.,Morikis, D.,Hausken, Z.E.,Coghlan, V.,Scott, J.D.,Jennings, P.A. (deposition date: 2006-06-10, release date: 2006-08-29, Last modification date: 2024-05-29)

Primary citation

Newlon, M.G.,Roy, M.,Morikis, D.,Carr, D.W.,Westphal, R.,Scott, J.D.,Jennings, P.A.
A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes.
Embo J., 20:1651-1662, 2001

PubMed Abstract: The specificity of intracellular signaling events is controlled, in part, by compartmentalization of protein kinases and phosphatases. The subcellular localization of these enzymes is often maintained by protein- protein interactions. A prototypic example is the compartmentalization of the cAMP-dependent protein kinase (PKA) through its association with A-kinase anchoring proteins (AKAPs). A docking and dimerization domain (D/D) located within the first 45 residues of each regulatory (R) subunit protomer forms a high affinity binding site for its anchoring partner. We now report the structures of two D/D-AKAP peptide complexes obtained by solution NMR methods, one with Ht31(493-515) and the other with AKAP79(392-413). We present the first direct structural data demonstrating the helical nature of the peptides. The structures reveal conserved hydrophobic interaction surfaces on the helical AKAP peptides and the PKA R subunit, which are responsible for mediating the high affinity association in the complexes. In a departure from the dimer-dimer interactions seen in other X-type four-helix bundle dimeric proteins, our structures reveal a novel hydrophobic groove that accommodates one AKAP per RIIalpha D/D.

PubMed: 11285229
DOI: 10.1093/emboj/20.7.1651

Experimental method

SOLUTION NMR