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Image Search Results
Journal: Nature
Article Title: Structure-function analysis of the SHOC2-MRAS-PP1C holophosphatase complex
doi: 10.1038/s41586-022-04928-2
Figure Lengend Snippet: a, An overview of the MD simulation system for the SHOC2 complex. b, Root-mean-square-deviation (RMSD) of the protein α-carbon throughout the simulation. c, Interaction fraction of contacting residue pairs between SHOC2 and PP1C. d, Interaction fraction of contacting residue pairs between SHOC2 and MRAS. e, Interaction fraction of contacting residue pairs between MRAS and PP1C. f, Local electron density map for T411 of SHOC2 (teal) and K147 of PP1CA (orange) and their neighboring residues (left) and SHOC2 N-terminal residues interacting with RVxF binding pocket of PP1c (right). The map (2Fo-Fc) is at 4.5 sigma. g, Sedimentation Velocity Analytical Ultracentrifugation (SV-AUC) analysis of PP1C binding to SHOC2 or MRAS-GppCp compared to PP1C alone, and with the presence of SHOC2 and MRAS-GppCp.
Article Snippet: The dialyzed protein was treated with 1mM EDTA, 20 units of Alkaline Phosphatase (Sigma, P0114) per mg of protein, 4X molar excess of
Techniques: Cryo-EM Sample Prep, Binding Assay, Sedimentation