1DEV

CRYSTAL STRUCTURE OF SMAD2 MH2 DOMAIN BOUND TO THE SMAD-BINDING DOMAIN OF SARA

Summary for 1DEV

• Entry DOI: 10.2210/pdb1dev/pdb
• Descriptor: MAD (mothers against decapentaplegic, Drosophila) homolog 2, Smad anchor for receptor activation (2 entities in total)
• Functional Keywords: beta sheet, three-helix bundle, signaling protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm : Q15796 O95405
• Total number of polymer chains: 4
• Total formula weight: 52817.75

Authors

Shi, Y.,Wu, G. (deposition date: 1999-11-15, release date: 2000-01-21, Last modification date: 2024-02-07)

Primary citation

Wu, G.,Chen, Y.G.,Ozdamar, B.,Gyuricza, C.A.,Chong, P.A.,Wrana, J.L.,Massague, J.,Shi, Y.
Structural basis of Smad2 recognition by the Smad anchor for receptor activation.
Science, 287:92-97, 2000

PubMed Abstract: 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.

PubMed: 10615055
DOI: 10.1126/science.287.5450.92

Experimental method

X-RAY DIFFRACTION (2.2 Å)