RACK1 (receptor for activated C-kinase 1) interactions with spectrin repeat elements.

摘要: Receptor for activated C-kinase 1 (RACK1) is an intracellular scaffolding protein involved in a multitude of signalling pathways. The cytoskeleton fundamental cell as it forms interconnected network regulatory proteins. Here, spectrin central component the actin-spectrin that serves docking surfaces cellular components. interaction between RACK1 and components spectrin, single repeats R16, R17 double repeat R1617 from α-spectrin chain were investigated by biosensor technology analysis. associated only weakly to R16 (KD  = 1.0 ± 0.5 × 10(-6)  M), about 20 times stronger  = 5.3 ± 0.7 × 10(-8)  M) 100  = 0.9 ± 0.3 × 10(-8)  M). Docking analysis showed while alone preferentially docked with its B-helix, through A-helix BC loop. mainly formed two different complex conformations. tangentially N/C-terminal or radially along groove on outer surface RACK1. These configurations could account slight increase entropic decrease enthalpic interactions R1617-RACK1 interaction, compared repeats. Our results suggest mode allows attach N/C part RACK inter-helical AB loops adopt limiting configurations.