Structural basis of Smad2 recognition by the Smad anchor for receptor activation Journal Article
| Authors: | Wu, G.; Chen, Y. G.; Ozdamar, B.; Gyuricza, C. A.; Chong, P. A.; Wrana, J. L.; Massague, J.; Shi, Y. G. |
| Article Title: | Structural basis of Smad2 recognition by the Smad anchor for receptor activation |
| Abstract: | The Smad proteins mediate transforming growth factor-beta (TGF beta) signaling from the transmembrane serine-threonine receptor kinases to the nucleus. The Smad anchor for receptor activation (SARA) recruits Smad2 to the TGF beta receptors for phosphorylation. The crystal structure of a Smad2 MH2 domain in complex with the Smad-binding domain (SBD) of SARA has been determined at 2.2 angstrom resolution. SARA SBD, in an extended conformation comprising a rigid coil, an alpha helix, and a beta strand, interacts with the beta sheet and the three-helix bundle of Smad2 Recognition between the SARA rigid coil and the Smad2 beta sheet is essential for specificity, whereas interactions between the SARA beta strand and the Smad2 three-helix bundle contribute significantly to binding affinity. Comparison of the structures between Smad2 and a comediator Smad suggests a model for how receptor-regulated Smads are recognized by the type I receptors. |
| Keywords: | proteins; specificity; complex; tgf-beta receptor |
| Journal Title: | Science |
| Volume: | 287 |
| Issue: | 5450 |
| ISSN: | 0036-8075 |
| Publisher: | American Association for the Advancement of Science |
| Date Published: | 2000-01-07 |
| Start Page: | 92 |
| End Page: | 97 |
| Language: | English |
| ACCESSION: | WOS:000084578400041 |
| DOI: | 10.1126/science.287.5450.92 |
| PROVIDER: | wos |
| PUBMED: | 10615055 |
| Notes: | Article -- Source: Wos |
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