Figure 2.

Structural Model of KLHL26‐CUL3 complex. (a) Our structural model is colored according to domain, depicting the predicted interaction with CUL3 mediated by the BACK and BTB domains. Residues outside of established domains by sequence comparison are colored white. Residues in the BTB domain that flank a site of additional sequence due to alternative splicing are circled. (b) Magnification of the BACK domain defines the location of R237 and its proximity to the CUL3 binding surface. (c). The electrostatic surface of KLHL26‐CUL3 interaction, wherein R237 is circled. (d) The analogous image of 2C for C237, wherein the electrostatic surface is more neutral and partially negative. (e) A 180° rotated view of the electrostatic surface of KLHL26‐CUL3 interaction; the gold circle marks the location of R237. (f) The positive patch on CUL3 is seen across from R237 (parts of KLHL26 that occlude the CUL3 surface are hidden). This patch is created by an HKH sequence whose sidechains fan out radially, contributing to a positive crescent‐shaped region, leaving the backbone oxygen atoms to make a negative surface patch