title: Evidence for an essential arginine recognition site on adenosine 3':5'-cyclic monophosphate-dependent protein kinase of rabbit skeletal muscle.
abstract: On the basis of the chemical and structural features of the amino acid sequences in the vicinities of phosphorylatable hydroxyamino acid residues in several of the well-known protein substrates for skeletal-muscle cyclic AMP-dependent protein kinase, it is hypothesized that the phosphorylatable residue at position i and arginine residue at position i-3 of these protein substrates are located on a peptide turn on the hydrophilic protein surface. It is further hypothesized that there is an arginine-recognition site near the active centre on the protein kinase. This site is essential for the function of cyclic AMP-dependent protein kinase, for, not only does it recognize specifically the exposed arginine residue of the protein substrate, but, more importantly, via the interaction with arginine-(i--3), it may help to steer the topologically adjacent serine-i into proper orientation on the nearby active centre for phosphorylation. Model-building and kinetic data that provide support for the proposed hypotheses are presented.
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D001120:Arginine / Q000494:pharmacology; D001224:Aspartic Acid / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D000242:Cyclic AMP / Q000378:metabolism; D007700:Kinetics; D008274:Magnesium / Q000378:metabolism; D010455:Peptides / Q000494:pharmacology; D011099:Polyglutamic Acid / Q000378:metabolism; D011107:Polylysine / Q000494:pharmacology; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases / Q000378:metabolism*
chemical_list: D010455:Peptides; D047428:Protein Kinase Inhibitors; D011107:Polylysine; D011099:Polyglutamic Acid; D001224:Aspartic Acid; D000255:Adenosine Triphosphate; D001120:Arginine; D000242:Cyclic AMP; D011494:Protein Kinases; D008274:Magnesium