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Updated: Aug 13, 2026

Photoactivated Localization Microscopy with Bimolecular Fluorescence Complementation (BiFC-PALM)
Published on: December 22, 2015
Structure of the Ras-binding domain of c-Raf-1 as determined by NMR spectroscopy and identification of the region
S D Emerson1, V S Madison, R E Palermo
1Roche Research Center, Hoffmann-La Roche Inc., Nutley, NJ 07110, USA.
Abstract:
The structure of the Ras-binding domain of human c-Raf-1 (residues 55 to 132) as determined in solution by NMR spectroscopy is presented. It consists of a five-stranded beta-sheet, a twelve residue alpha-helix, and an additional one-turn helix. The fold belongs to a known family whose members include ubiquitin and protein G. The surface of Raf55-132 that interacts with Ras has been identified by resonance perturbation mapping. The binding site is a spatially contiguous patch comprised of the two-N-terminal beta-strands, the loop between them, and the C-terminal end of the alpha-helix. A model of the Raf-Ras complex is presented, which was derived by analogy to the complex between protein G and a Fab fragment of IgG. In the model, edge beta-strands of each protein align in an antiparallel orientation, forming a unified beta-sheet, and side chains from both proteins are able to participate in ionic and hydrophobic interactions at the interface.
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