Myristoylation-regulated Direct Interaction Between Calcium-bound Calmodulin and N-terminal Region of pp60v-src

pp60v-src tyrosine protein kinase was suggested to interact with Ca2+-bound calmodulin (Ca2+/CaM) through the N-terminal region based on its structural similarities to CAP-23/NAP-22, a myristoylated neuron-specific protein, whose myristoyl group is essential for interaction with Ca2+/CaM; (1) the N...

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Veröffentlicht in:	Journal of molecular biology 2004-04, Vol.338 (1), p.169-180
Hauptverfasser:	Hayashi, Nobuhiro, Nakagawa, Chisako, Ito, Yutaka, Takasaki, Akihiko, Jinbo, Yuji, Yamakawa, Yoshinori, Titani, Koiti, Hashimoto, Keiichiro, Izumi, Yoshinobu, Matsushima, Norio
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites Calcium - metabolism calmodulin Calmodulin - chemistry Calmodulin - metabolism Humans Mass Spectrometry Myristic Acid - metabolism myristoylation Nuclear Magnetic Resonance, Biomolecular Oncogene Protein pp60(v-src) - chemistry Oncogene Protein pp60(v-src) - metabolism Peptide Fragments - chemistry Peptide Fragments - metabolism Phosphorylation pp60v-src Protein Binding Protein Conformation Protein Kinase C - pharmacology protein–protein interaction small-angle X-ray scattering X-Ray Diffraction
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