2h9r

From Proteopedia

Revision as of 20:22, 12 November 2007

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)

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

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