期刊
EMBO JOURNAL
卷 20, 期 7, 页码 1651-1662出版社
OXFORD UNIV PRESS
DOI: 10.1093/emboj/20.7.1651
关键词
AKAP; PKA; NMR; signal transduction; subcellular localization
资金
- NCI NIH HHS [CA09523, T32 CA009523] Funding Source: Medline
- NICHD NIH HHS [R01 HD036408, R01 HD036408-08] Funding Source: Medline
- NIDDK NIH HHS [DK44239, DK5444, P01 DK044239] Funding Source: Medline
The specificity of intracellular signaling events is controlled, in part, by compartmentalization of protein kinases and phosphatases, The subcellular localization of these enzymes is often maintained by protein-protein interactions. A prototypic example is the compartmentalization of the cAMP-dependent protein kinase (PKA) through its association with A-kinase anchoring proteins (AKAPs), A docking and dimerization domain (D/D) located within the first 45 residues of each regulatory (R) subunit protomer forms a high affinity binding site for its anchoring partner. We now report the structures of two D/D-AKAP peptide complexes obtained by solution NMR methods, one with Ht31(493-515) and the other with AKAP79(392-413), We present the first direct structural data demonstrating the helical nature of the peptides, The structures reveal conserved hydrophobic interaction surfaces on the helical AKAP peptides and the PKA R subunit, which are responsible for mediating the high affinity association in the complexes. In a departure from the dimer-dimer interactions seen in other X-type four-helix bundle dimeric proteins, our structures reveal a novel hydrophobic groove that accommodates one AKAP per RII alpha D/D.
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