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Domain binding and function: The MH2 domain of R-Smads allows the interaction with the Smad binding domain (SBD) of SARA. SARA recruits R-Smads to the type I TGFbeta receptor, and this is believed to be stabilized by a charge-mediated interaction between the MH2 domain and the cytoplasmic domain of the type I TGFbeta-R. The MH2 of the co-Smad, Smad4, appears to be responsible for homooligomerization of Smad4 trimers into disk-like structures and heterooligomerization between Smad4 trimers and Smad2 trimer disks. Mutations in the Smad4 trimer interface disrupt homo-oligomerization and result in inactivation of Smad4 tumor suppression function observed in pancreatic carcinomas and other cancers.
Structure Reference: Wu, G. et al. (2000) Science 287(5450), 92À97.
Examples of Domain Proteins:
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