Pseudokinases kinase suppressor of Ras 1 and 2 (KSR1/2) are scaffolds that bridge RAF isoforms and their substrate, mitogen-activated protein kinase kinase (MEK). They dimerize with kinase-competent RAFs (ARAF, BRAF and CRAF) to stimulate catalysis allosterically []. This entry represents the N-terminal helical hairpin which, together with the SAM-like domain () constitutes the N-terminal regulatory region that mediates heterodimerization of BRAF with KSR1. Additionally, MEK binding to the kinase domain of KSR1 asymmetrically drives BRAF-KSR1 heterodimerization, resulting in the concomitant stimulation of BRAF catalytic activity towards free MEK molecules [].
Pseudokinases kinase suppressor of Ras 1 and 2 (KSR1/2) are scaffolds that bridge RAF isoforms and their substrate, mitogen-activated protein kinase kinase (MEK). They dimerize with kinase-competent RAFs (ARAF, BRAF and CRAF) to stimulate catalysis allosterically []. This entry represents the N-terminal helical hairpin which, together with the SAM-like domain () constitutes the N-terminal regulatory region that mediates heterodimerization of BRAF with KSR1. Additionally, MEK binding to the kinase domain of KSR1 asymmetrically drives BRAF-KSR1 heterodimerization, resulting in the concomitant stimulation of BRAF catalytic activity towards free MEK molecules [].
