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CRYSTAL STRUCTURE OF SMAD2 MH2 DOMAIN BOUND TO THE SMAD-BINDING DOMAIN OF SARA
OverviewOverview
The Smad proteins mediate transforming growth factor-beta (TGFbeta), signaling from the transmembrane serine-threonine receptor kinases to the, nucleus. The Smad anchor for receptor activation (SARA) recruits Smad2 to, the TGFbeta 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.
DiseaseDisease
Known diseases associated with this structure: Anderson disease OMIM:[607690], Chylomicron retention disease OMIM:[607690], Chylomicron retention disease with Marinesco-Sjogren syndrome OMIM:[607690], Mowat-Wilson syndrome OMIM:[605802]
About this StructureAbout this Structure
1DEV is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of Smad2 recognition by the Smad anchor for receptor activation., Wu G, Chen YG, Ozdamar B, Gyuricza CA, Chong PA, Wrana JL, Massague J, Shi Y, Science. 2000 Jan 7;287(5450):92-7. PMID:10615055
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