SARASmad anchor for receptor activation (SARA) |
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| SMART accession number: | SM01422
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| Description: |
Smad proteins mediate transforming growth factor-beta (TGF-beta) signaling from the transmembrane serine-threonine receptor kinases to the nucleus PMID:10615055. SARA recruits Smad2 to the TGF-beta receptors for phosphorylation PMID:10615055. |
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| Family alignment: |
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There are 0 SARA domains in 0 proteins in SMART's nrdb database.
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Cellular role (predicted cellular role)
Cellular role: signalling
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Wu G et al.
- Structural basis of Smad2 recognition by the Smad anchor for receptor activation.
- Science. 2000; 287: 92-7
- Display abstract
The Smad proteins mediate transforming growth factor-beta (TGFbeta) signalingfrom the transmembrane serine-threonine receptor kinases to the nucleus. The Smadanchor for receptor activation (SARA) recruits Smad2 to the TGFbeta receptors forphosphorylation. 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 ofSmad2. Recognition between the SARA rigid coil and the Smad2 beta sheet isessential 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 modelfor how receptor-regulated Smads are recognized by the type I receptors.
Structure (3D structures containing this domain)3D Structures of SARA domains in PDB
| PDB code | Main view | Title | | 1dev |  | CRYSTAL STRUCTURE OF SMAD2 MH2 DOMAIN BOUND TO THE SMAD-BINDING DOMAIN OF SARA |
| 1mk2 |  | SMAD3 SBD complex |
Links (links to other resources describing this domain)
