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| {{STRUCTURE_2izy| PDB=2izy | SCENE= }} | | {{STRUCTURE_2izy| PDB=2izy | SCENE= }} |
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| '''MOLECULAR BASIS OF AKAP SPECIFICITY FOR PKA REGULATORY SUBUNITS'''
| | ===MOLECULAR BASIS OF AKAP SPECIFICITY FOR PKA REGULATORY SUBUNITS=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17081989}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17081989 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17081989}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Rii]] | | [[Category: Rii]] |
| [[Category: Transferase]] | | [[Category: Transferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:08:22 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:38:16 2008'' |
