Defining Protein−Protein Interactions Using Site-Directed Spin-Labeling: The Binding of Protein Kinase C Substrates to Calmodulin

EPR spectroscopy was used to examine protein−protein interactions between calmodulin and spin-labeled peptides based on the protein kinase C substrate domains of the myristoylated alanine rich C kinase substrate (MARCKS) and neuromodulin. When bound to calmodulin, the C- and N-terminal ends of a 25...

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Veröffentlicht in:	Biochemistry (Easton) 1996-10, Vol.35 (41), p.13272-13276
Hauptverfasser:	Qin, Zhihai, Wertz, Stacey L, Jacob, Jaison, Savino, Yoko, Cafiso, David S
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Binding Sites Calmodulin - chemistry Calmodulin - metabolism Electron Spin Resonance Spectroscopy GAP-43 Protein In Vitro Techniques Intracellular Signaling Peptides and Proteins Membrane Glycoproteins - chemistry Membrane Glycoproteins - metabolism Membrane Proteins Models, Molecular Molecular Sequence Data Myristoylated Alanine-Rich C Kinase Substrate Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - metabolism Peptide Fragments - chemistry Peptide Fragments - metabolism Protein Binding Protein Conformation Protein Kinase C - chemistry Protein Kinase C - metabolism Proteins - chemistry Proteins - metabolism Spin Labels Substrate Specificity
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