Backbone NMR resonance assignment of the catalytic subunit of cAMP-dependent protein kinase A in complex with AMP-PNP.
The catalytic subunit of protein kinase A is involved with a number of signal transduction pathways and has been used as a benchmark to study the structural biology and biochemistry for the entire kinase family of enzymes. Here, we report the backbone assignment of the intact 41 kDa catalytic subunit bound to AMP-PNP.
Masterson
Larry R
LR
Department of Chemistry and Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
Shi
Lei
L
Tonelli
Marco
M
Mascioni
Alessandro
A
Mueller
Michael M
MM
Veglia
Gianluigi
G
D000266:Adenylyl Imidodiphosphate / Q000737:chemistry*; D000595:Amino Acid Sequence; D001665:Binding Sites; D002247:Carbon Isotopes / Q000737:chemistry; D002384:Catalysis; D017868:Cyclic AMP-Dependent Protein Kinases / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000737:chemistry; D009587:Nitrogen Isotopes / Q000737:chemistry; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D011522:Protons
D002247:Carbon Isotopes; D046912:Multiprotein Complexes; D009587:Nitrogen Isotopes; D021122:Protein Subunits; D011522:Protons; D000266:Adenylyl Imidodiphosphate; D017868:Cyclic AMP-Dependent Protein Kinases