2izx
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MOLECULAR BASIS OF AKAP SPECIFICITY FOR PKA REGULATORY SUBUNITS
OverviewOverview
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, ... [(full description)]
About this StructureAbout this Structure
2IZX is a [Single protein] structure of sequence from [Homo sapiens] with DTD as [ligand]. Active as [cAMP-dependent protein kinase], with EC number [2.7.11.11]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Molecular basis of AKAP specificity for PKA regulatory subunits., Gold MG, Lygren B, Dokurno P, Hoshi N, McConnachie G, Tasken K, Carlson CR, Scott JD, Barford D, Mol Cell. 2006 Nov 3;24(3):383-95. PMID:17081989
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