Identification of the interface between cGMP-dependent protein kinase Ibeta and its interaction partners TFII-I and IRAG reveals a common interaction motif.

Casteel, Darren E

Identification of the interface between cGMP-dependent protein kinase Ibeta and its interaction partners TFII-I and IRAG reveals a common interaction motif. [electronic resource] - The Journal of biological chemistry Nov 2005 - 38211-8 p. digital

Publication Type: Journal Article; Research Support, N.I.H., Extramural

0021-9258

10.1074/jbc.M507021200 doi


Alternative Splicing
Amino Acid Motifs
Amino Acid Sequence
Animals
COS Cells
Calcium Channels--chemistry
Cattle
Cell Line
Chlorocebus aethiops
Cloning, Molecular
Cyclic GMP-Dependent Protein Kinases--metabolism
DNA--chemistry
Dimerization
Electrophoresis, Polyacrylamide Gel
Glutathione Transferase--metabolism
Humans
Immunoblotting
Inositol 1,4,5-Trisphosphate Receptors
Leucine--chemistry
Membrane Proteins
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation
Phosphoproteins--metabolism
Protein Binding
Protein Structure, Secondary
Protein Structure, Tertiary
Receptors, Cytoplasmic and Nuclear--chemistry
Signal Transduction
Static Electricity
Transcription Factors, TFII--metabolism
Transcription, Genetic
Transfection