2ezw
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(New page: 200px<br /><applet load="2ezw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ezw" /> '''Solution structure of the docking and dimeri...)
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Revision as of 08:08, 21 November 2007
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Solution structure of the docking and dimerization domain of the type I alpha regulatory subunit of protein kinase A (RIalpha D/D)
Overview
The subcellular localization of cAMP-dependent protein kinase (PKA) occurs, through interaction with A-Kinase Anchoring Proteins (AKAPs). AKAPs bind, to the PKA regulatory subunit dimer of both type Ialpha and type IIalpha, (RIalpha and RIIalpha). RIalpha and RIIalpha display characteristic, localization within different cell types, which is maintained by, interaction of AKAPs with the N-terminal dimerization and docking domain, (D/D) of the respective regulatory subunit. Previously, we reported the, solution structure of RIIa D/D module, both free and bound to AKAPs. We, have now solved the solution structure of the dimerization and docking, domain of the type Ialpha regulatory dimer subunit (RIalpha D/D). RIalpha, D/D is a compact docking module, with unusual interchain disulfide bonds, that help maintain the AKAP interaction surface. In contrast to the, shallow hydrophobic groove for AKAP binding across the surface of the, RIIalpha D/D dimeric interface, the RIalpha D/D module presents a deep, cleft for proposed AKAP binding. RIalpha and RIIalpha D/D interaction, modules present drastically differing dimeric topographies, despite a, conserved X-type four-helix bundle structure.
About this Structure
2EZW is a Single protein structure of sequence from Bos taurus. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
Related protein-protein interaction modules present drastically different surface topographies despite a conserved helical platform., Banky P, Roy M, Newlon MG, Morikis D, Haste NM, Taylor SS, Jennings PA, J Mol Biol. 2003 Jul 25;330(5):1117-29. PMID:12860132
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