3IM3

Crystal structure of PKA RI alpha dimerization/docking domain

Summary for 3IM3

• Entry DOI: 10.2210/pdb3im3/pdb
• Related: 3IM4
• Descriptor: cAMP-dependent protein kinase type I-alpha regulatory subunit, FORMIC ACID (3 entities in total)
• Functional Keywords: helix-turn-helix, acetylation, camp, camp-binding, disulfide bond, nucleotide-binding, phosphoprotein, structural protein, signaling protein
• Biological source: Bos taurus (bovine)
• Total number of polymer chains: 1
• Total formula weight: 6098.03

Authors

Sarma, G.N.,Kinderman, F.S.,Kim, C.,von Daake, S.,Taylor, S.S. (deposition date: 2009-08-09, release date: 2010-02-02, Last modification date: 2024-11-20)

Primary citation

Sarma, G.N.,Kinderman, F.S.,Kim, C.,von Daake, S.,Chen, L.,Wang, B.C.,Taylor, S.S.
Structure of D-AKAP2:PKA RI Complex: Insights into AKAP Specificity and Selectivity
Structure, 18:155-166, 2010

PubMed Abstract: A-kinase anchoring proteins (AKAPs) regulate cyclic AMP-dependent protein kinase (PKA) signaling in space and time. Dual-specific AKAP 2 (D-AKAP2) binds to the dimerization/docking (D/D) domain of both RI and RII regulatory subunits of PKA with high affinity. Here we have determined the structures of the RIalpha D/D domain alone and in complex with D-AKAP2. The D/D domain presents an extensive surface for binding through a well-formed N-terminal helix, and this surface restricts the diversity of AKAPs that can interact. The structures also underscore the importance of a redox-sensitive disulfide in affecting AKAP binding. An unexpected shift in the helical register of D-AKAP2 compared to the RIIalpha:D-AKAP2 complex structure makes the mode of binding to RIalpha novel. Finally, the comparison allows us to deduce a molecular explanation for the sequence and spatial determinants of AKAP specificity.

PubMed: 20159461
DOI: 10.1016/j.str.2009.12.012

Experimental method

X-RAY DIFFRACTION (2 Å)