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. 2021 Feb 19;12:1176. doi: 10.1038/s41467-021-21422-x

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© This is a U.S. Government work and not under copyright protection in the US; foreign copyright protection may apply 2021

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Fig. 2 — a Superposition of KRAS-RBD structure (light blue) with KRAS-RBDCRD structure shows conformational differences in RBD. The structural superposition was carried out by aligning atoms in KRAS in both structures. b Enlarged view of RBD showing conformational differences that occur when it binds to KRAS as RBD vs. RBDCRD. c Schematic representation of the KRAS-RBD interaction interface, as identified by PDBSum (http://www.ebi.ac.uk/pdbsum/). The interactions are colored using the following notations: hydrogen bonds—solid blue lines, salt bridges—solid red lines, non-bonded contacts—striped orange lines (width of the striped line is proportional to the number of atomic contacts). d, e Enlarged view of the KRAS-RBD interaction interface formed by residues present in the d switch-I region (magenta), and e β2 strand (residues present at the end of the switch-I region) of KRAS. The nucleotide GMPPNP and residues that participate in the protein–protein interaction are shown in stick representation. Dashed black lines indicate intermolecular hydrogen bonds and salt bridges. f Steady-state binding isotherms derived from the SPR data for different point mutants of RBDCRD binding to KRAS-GMPPNP. g A bar graph showing binding affinity (K_D) obtained using the SPR data shown in f for point mutants of RBDCRD located at the KRAS-RBD interface. The K_D values are reported as the mean ± standard deviation from multiple replicates; WT (n = 17), R59A (n = 5), N64A (n = 5), Q66A (n = 8), R89L (n = 4), and F130E (n = 10). Source data are provided as a Source Data file. h Amino acid sequence alignment of residues present in the RAS-binding domain (RBD) of human RAF1, BRAF, and ARAF. Fully and partially conserved residues among the RAF isoforms are highlighted in red and yellow, respectively. The secondary structure of RAF1(RBD) is shown above the alignment. The RBD residues that are involved in the interaction with KRAS, CRD, and the linker region are indicated below the alignment with upright triangles, ovals and inverted triangles, respectively.