Structural Basis of Smad1 Activation by Receptor Kinase Phosphorylation

Phosphorylation of Smad1 at the conserved carboxyl terminal SVS sequence activates BMP signaling. Here we report the crystal structure of the Smad1 MH2 domain in a conformation that reveals the structural effects of phosphorylation and a molecular mechanism for activation. Within a trimeric subunit...

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Veröffentlicht in:	Molecular cell 2001-12, Vol.8 (6), p.1303-1312
Hauptverfasser:	Qin, Bin Y, Chacko, Benoy M, Lam, Suvana S, de Caestecker, Mark P, Correia, John J, Lin, Kai
Format:	Artikel
Sprache:	eng
Schlagworte:	Allosteric Regulation Amino Acid Sequence Binding Sites Cell Line Chromatography, Gel Crystallography, X-Ray DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Models, Biological Models, Molecular Molecular Sequence Data Phosphorylation Protein Binding Protein Structure, Quaternary Protein Structure, Tertiary Protein Subunits Sequence Alignment Signal Transduction Smad Proteins Structure-Activity Relationship Substrate Specificity Trans-Activators - chemistry Trans-Activators - genetics Trans-Activators - metabolism Transcription, Genetic Ultracentrifugation
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