Rearrangements in a hydrophobic core region mediate cAMP action in the regulatory subunit of PKA

cAMP-dependent protein kinase (PKA) forms an inactive heterotetramer of two regulatory (R; with two cAMP-binding domains A and B each) and two catalytic (C) subunits. Upon the binding of four cAMP molecules to the R dimer, the monomeric C subunits dissociate. Based on sequence analysis of cyclic nuc...

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Veröffentlicht in:	Biological chemistry 2005-07, Vol.386 (7), p.623-631
Hauptverfasser:	Hahnefeld, Claudia, Moll, Daniela, Goette, Maik, Herberg, Friedrich W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence cAMP-dependent protein kinase Circular Dichroism Cyclic AMP - physiology Cyclic AMP-Dependent Protein Kinases - chemistry Cyclic AMP-Dependent Protein Kinases - physiology exchange protein directly activated by cAMP Molecular Sequence Data Mutagenesis, Site-Directed Sequence Homology, Amino Acid Surface Plasmon Resonance
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