2h9r | pdb_00002h9r
Docking and dimerization domain (D/D) of the regulatory subunit of the Type II-alpha cAMP-dependent protein kinase A associated with a Peptide derived from an A-kinase anchoring protein (AKAP)
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Overview
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 RIIalpha D/D.
About this Structure
2H9R is a Protein complex structure of sequences from Rattus norvegicus. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes., Newlon MG, Roy M, Morikis D, Carr DW, Westphal R, Scott JD, Jennings PA, EMBO J. 2001 Apr 2;20(7):1651-62. PMID:11285229
Page seeded by OCA on Fri Feb 15 17:30:43 2008
