Dissecting the Cooperative Reassociation of the Regulatory and Catalytic Subunits of cAMP-dependent Protein Kinase ROLE OF Trp-196 IN THE CATALYTIC SUBUNIT
作者： Robin M. Gibson , Susan S. Taylor
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摘要: The catalytic (C) subunit of cAMP-dependent protein kinase requires two distinct surfaces to form a stable complex with its physiological inhibitors, the regulatory (R) subunits and heat-stable inhibitors. In addition substrate-like segment that is common both R peripheral recognition site, PRS2. This surface comprised essential phosphorylation Thr-197, His-87, Trp-196, several surrounding basic residues. To probe role Trp-196 in R, was replaced Arg Ala. Although rC(W196A) rC(W196R) were inhibited readily cAMP-free they failed an holoenzyme native under conditions which wild-type formed readily. Pairing mutant forms lacking domain B or having defects cAMP binding sites A highlighted importance conformation and, particular, accessibility site A. One these mutants, rR(R333K), defect absence cAMP. However, unlike holoenzyme, this active.
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