Fig. 6: Structure-based assessment of RALGAP variants.
From: Structure and mechanism of the RalGAP tumor suppressor complex
a Mapping and structure-based classification of RALGAPA2 and RALGAPB variants reported more than once in uterine and skin cancer patients. b Interaction of RGα2 catalytic helix residue R1738 with E97 of RalA. c Close-up of the β-hug/RGα2 binding site with the positions of patient variants shown as spheres. d Representation of the RGβ N-terminal homodimerization interface with the amino acids at positions of patient variants shown as sticks. e Stabilization of the RGβhug binding site of RGα2 by N943.
