| Literature DB >> 17081990 |
Francis S Kinderman1, Choel Kim, Sventja von Daake, Yuliang Ma, Bao Q Pham, Glen Spraggon, Nguyen-Huu Xuong, Patricia A Jennings, Susan S Taylor.
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.Entities:
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Year: 2006 PMID： 17081990 PMCID： PMC1855097 DOI： 10.1016/j.molcel.2006.09.015
Source DB: PubMed Journal: Mol Cell ISSN： 1097-2765 Impact factor: 17.970