2IZY

Molecular Basis of AKAP Specificity for PKA Regulatory Subunits

Summary for 2IZY

• Entry DOI: 10.2210/pdb2izy/pdb
• Descriptor: CAMP-DEPENDENT PROTEIN KINASE REGULATORY SUBUNIT II (2 entities in total)
• Functional Keywords: d/d, rii, pka, camp, kinase, acetylation, transferase, camp- binding, phosphorylation, nucleotide-binding
• Biological source: MUS MUSCULUS (MOUSE)
• Total number of polymer chains: 8
• Total formula weight: 51105.91

Authors

Gold, M.G.,Lygren, B.,Dokurno, P.,Hoshi, N.,McConnachie, G.,Tasken, K.,Carlson, C.R.,Scott, J.D.,Barford, D. (deposition date: 2006-07-27, release date: 2006-11-13, Last modification date: 2024-05-08)

Primary citation

Gold, M.G.,Lygren, B.,Dokurno, P.,Hoshi, N.,Mcconnachie, G.,Tasken, K.,Carlson, C.R.,Scott, J.D.,Barford, D.
Molecular Basis of Akap Specificity for Pka Regululatory Subunits
Mol.Cell, 24:383-, 2006

PubMed Abstract: Localization of cyclic AMP (cAMP)-dependent protein kinase (PKA) by A kinase-anchoring proteins (AKAPs) restricts the action of this broad specificity kinase. The high-resolution crystal structures of the docking and dimerization (D/D) domain of the RIIalpha regulatory subunit of PKA both in the apo state and in complex with the high-affinity anchoring peptide AKAP-IS explain the molecular basis for AKAP-regulatory subunit recognition. AKAP-IS folds into an amphipathic alpha helix that engages an essentially preformed shallow groove on the surface of the RII dimer D/D domains. Conserved AKAP aliphatic residues dominate interactions to RII at the predominantly hydrophobic interface, whereas polar residues are important in conferring R subunit isoform specificity. Using a peptide screening approach, we have developed SuperAKAP-IS, a peptide that is 10,000-fold more selective for the RII isoform relative to RI and can be used to assess the impact of PKA isoform-selective anchoring on cAMP-responsive events inside cells.

PubMed: 17081989
DOI: 10.1016/J.MOLCEL.2006.09.006

Experimental method

X-RAY DIFFRACTION (2.2 Å)