2HWN

Crystal Structure of RII alpha Dimerization/Docking domain of PKA bound to the D-AKAP2 peptide

Summary for 2HWN

• Entry DOI: 10.2210/pdb2hwn/pdb
• Related: 1R2A
• Descriptor: cAMP-dependent protein kinase type II-alpha regulatory subunit, A Kinase binding peptide, GLYCEROL, ... (4 entities in total)
• Functional Keywords: pka, akap, dimerization/docking, d/d, regulatory subunit, transferase
• Biological source: Rattus norvegicus (Norway rat)
• Total number of polymer chains: 6
• Total formula weight: 26474.63

Authors

Kinderman, F.,Kim, C. (deposition date: 2006-08-01, release date: 2006-11-21, Last modification date: 2024-02-14)

Primary citation

Kinderman, F.S.,Kim, C.,von Daake, S.,Ma, Y.,Pham, B.Q.,Spraggon, G.,Xuong, N.H.,Jennings, P.A.,Taylor, S.S.
A Dynamic Mechanism for AKAP Binding to RII Isoforms of cAMP-Dependent Protein Kinase.
Mol.Cell, 24:397-408, 2006

PubMed Abstract: A kinase-anchoring proteins (AKAPs) target PKA to specific microdomains by using an amphipathic helix that docks to N-terminal dimerization and docking (D/D) domains of PKA regulatory (R) subunits. To understand specificity, we solved the crystal structure of the helical motif from D-AKAP2, a dual-specific AKAP, bound to the RIIalpha D/D domain. The 1.6 Angstrom structure reveals how this dynamic, hydrophobic docking site is assembled. A stable, hydrophobic docking groove is formed by the helical interface of two RIIalpha protomers. The flexible N terminus of one protomer is then recruited to the site, anchored to the peptide through two essential isoleucines. The other N terminus is disordered. This asymmetry provides greater possibilities for AKAP docking. Although there is strong discrimination against RIalpha in the N terminus of the AKAP helix, the hydrophobic groove discriminates against RIIalpha. RIalpha, with a cavity in the groove, can accept a bulky tryptophan, whereas RIIalpha requires valine.

PubMed: 17081990
DOI: 10.1016/j.molcel.2006.09.015

Experimental method

X-RAY DIFFRACTION (1.6 Å)