RAB6 binding domain (RBD) found in kinesin-like protein KIF20A, and similar proteins
KIF20A, also called GG10_2, or mitotic kinesin-like protein 2 (MKlp2), or Rab6-interacting kinesin-like protein, or rabkinesin-6, is a mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1, it is involved in recruitment of PLK1 (polo-like kinase 1) to the central spindle. KIF20A interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. It may act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. KIF20A has a microtubule plus end-directed motility. This model corresponds to RAB6 binding domain (RBD) of KIF20A. KIF20A-RBD is a dimer composed of two parallel alpha helices that form a right-handed coiled-coil additionally stabilized by an inter-helical cysteine bridge.
Feature 1:RAB6 binding site [polypeptide binding site]
Comment: KIF20A-RAB6-binding domain (KIF20A-RBD) is a dimer composed of parallel helices that form a right-handed coiled-coil stabilized by an inter-helical cysteine bridge and two RAB6 molecules bind on opposite sides of the dimer
Structure:5LEF: Mus musculus RAB6 binding domain (RBD) of kinesin family protein KIF20A forms a dimer with each monomer binding one RAB6; contacts at 4A - View structure with Cn3D