The TβR-I Pre-Helix Extension Is Structurally Ordered in the Unbound Form and Its Flanking Prolines Are Essential for Binding

• Published in: Journal of molecular biology Vol. 412; no. 4; pp. 601 - 618
• Main Authors: Zuniga, Jorge E., Ilangovan, Udayar, Mahlawat, Pardeep, Hinck, Cynthia S., Huang, Tao, Groppe, Jay C., McEwen, Donald G., Hinck, Andrew P.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier Ltd 30.09.2011
• Subjects: Amino Acid Sequence; bone morphogenetic proteins; cis-proline; cooperative binding; Crystallography, X-Ray; epithelial cells; Humans; Isoleucine - chemistry; Isoleucine - physiology; Models, Molecular; Molecular Sequence Data; nuclear magnetic resonance spectroscopy; Nuclear Magnetic Resonance, Biomolecular; Proline - chemistry; Proline - metabolism; Proline - physiology; Protein Binding - physiology; Protein Interaction Domains and Motifs; Protein Serine-Threonine Kinases - chemistry; Protein Serine-Threonine Kinases - metabolism; Protein Structure, Quaternary; Protein Structure, Secondary - physiology; Receptor, Transforming Growth Factor-beta Type I; receptors; Receptors, Transforming Growth Factor beta - chemistry; Receptors, Transforming Growth Factor beta - metabolism; reporter genes; Sequence Homology, Amino Acid; specificity; TGF-β; transforming growth factor beta; Transforming Growth Factor beta1 - metabolism; type I receptor; BMP; NOE; GDF; BMPR-I; SA; PDB; RDC; 3D; SPR; IPAP; cis-proline; TβR-II; R-Smad; type I receptor; specificity; TGF-β; NOESY; BMPR-Ia ED; HSQC; TβR-I ED; TβR-II ED; WT; TβR-I; cooperative binding

Transforming growth factor β isoforms (TGF-β) are among the most recently evolved members of a signaling superfamily with more than 30 members. TGF-β play vital roles in regulating cellular growth and differentiation, and they signal through a highly restricted subset of receptors known as TGF-β typ...