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)

Citation:
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.
PDB ID: 2H9RDownload
MMDB ID: 41011
PDB Deposition Date: 2006/6/10
Updated in MMDB: 2007/10
Experimental Method:
solution nmr
Source Organism:
Rattus norvegicus
Similar Structures:
Molecular Components in 2H9R
Label Count Molecule
Proteins (3 molecules)
2
Camp-dependent Protein Kinase Type Ii-alpha Regulatory Subunit(Gene symbol: Prkar2a)
Molecule annotation
1
22-mer From A-kinase Anchor Protein 5(Gene symbol: AKAP5)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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