Fig. 3: Structural and mutational analyses of the role of linker residues present between RBD and CRD in the KRAS-RBDCRD structure. | Nature Communications

Fig. 3: Structural and mutational analyses of the role of linker residues present between RBD and CRD in the KRAS-RBDCRD structure.

From: KRAS interaction with RAF1 RAS-binding ___domain and cysteine-rich ___domain provides insights into RAS-mediated RAF activation

Fig. 3

a The surface representation of RBDCRD showing how linker residues connect RBD and CRD, resulting in the formation of an extended structure. The lower panel shows the region of RBDCRD that interacts with KRAS (colored gray), suggesting RBD as well as CRD interact with KRAS. b Amino acid sequence alignment of residues present in the linker region of human RAF1, BRAF, and ARAF. Residues that are involved in the interaction with RBD and CRD are indicated below the alignment with stars and oval, respectively. c Enlarged view of the RBD and CRD interaction interface formed by residues present in the linker region. Residues that participate in interdomain interaction are shown in stick representation. A lone hydrogen bond is shown as a black dashed line. d Steady-state binding isotherms derived from the SPR data for the WT-RBDCRD and L136A mutant present in the linker region binding to KRAS-GMPPNP.

Back to article page