Journal
STRUCTURE
Volume 18, Issue 2, Pages 155-166Publisher
CELL PRESS
DOI: 10.1016/j.str.2009.12.012
Keywords
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Funding
- NIH [DK054441, GM34921]
- American Heart Association postdoctoral fellowship [0825041 F]
- Director, Office of Science, Office of Basic Energy Sciences, of the U.S. Department of Energy [DE-AC02-05CH11231, DE-AC02-06CH11357]
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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 RI alpha 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 RII alpha:D-AKAP2 complex structure makes the mode of binding to RI alpha novel. Finally, the comparison allows us to deduce a molecular explanation for the sequence and spatial determinants of AKAP specificity.
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