The Role of Unstructured Highly Charged Regions on the Stability and Specificity of Dimerization of Two-Stranded α-Helical Coiled-Coils: Neck Region of Kinesin-Like Motor Protein Kif3A

Abstract

Many of the kinesin-like motor proteins function as homo or heterodimeric molecules. Interestingly, many of these molecules have conserved regions following their globular head domains referred to as the neck and linker regions [1]. The neck region is thought to play a critical role in motor function, while the linker region is thought to specify heterodimer formation for the heterodimeric motor proteins [2]. This study was designed to elucidate whether preferential heterodimer formation can be attributed to the linker regions, rich in charged residues that follow the neck region of some kinesin-like motor proteins.