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The human transcription factor, RFX1, is found to belong to the winged-helix family of DNA binding proteins, despite an absence of significant sequence similarity. Even more surprising is the very different mode of DNA binding as compared with previously characterized winged-helix proteins that bind to B-form DNA.
The U1A protein regulates the activity of poly(A) polymerase by interacting with an RNA element in the 3′ untranslated region of its mRNA. The structure of the trimolecular complex made up of two U1A molecules bound to the target RNA explains the cooperative regulation in this system.
The mechanism by which cells recognize misfolded proteins in the endoplasmic reticulum has been defined at the cell biological level. The enzyme UDP-glucose:glycoprotein glucosyltransferase identifies and specifically glucosylates misfolded domains within a multi-domain protein.
The tide of the blood coagulation cascade turns by a switch in thrombin specificity. Two new structures reveal how thrombomodulin's EGF domains flip the switch by blocking old substrates and docking new ones.
