Rotational coupling of the transmembrane and kinase domains of the Neu receptor tyrosine kinase

Ligand binding to receptor tyrosine kinases (RTKs) regulates receptor dimerization and activation of the kinase domain. To examine the role of the transmembrane domain in regulation of RTK activation, we have exploited a simplified transmembrane motif, [VVVEVVV](n), previously shown to activate the...

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Veröffentlicht in:	Molecular biology of the cell 2000-10, Vol.11 (10), p.3589-3599
Hauptverfasser:	Bell, C A, Tynan, J A, Hart, K C, Meyer, A N, Robertson, S C, Donoghue, D J
Format:	Artikel
Sprache:	eng
Schlagworte:	3T3 Cells Amino Acid Sequence Animals Base Sequence Cercopithecus aethiops COS Cells Dimerization Ligands Mice Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Oligodeoxyribonucleotides - chemistry Oligodeoxyribonucleotides - metabolism Protein Conformation Receptor Protein-Tyrosine Kinases - chemistry Receptor Protein-Tyrosine Kinases - genetics Receptor Protein-Tyrosine Kinases - metabolism Receptor, ErbB-2 - chemistry Receptor, ErbB-2 - genetics Receptor, ErbB-2 - metabolism Receptor, Platelet-Derived Growth Factor beta - chemistry Receptor, Platelet-Derived Growth Factor beta - genetics Receptor, Platelet-Derived Growth Factor beta - metabolism Transcription, Genetic
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