Abstract : Kapβ1 transfers protein molecules from the cytoplasm cells to the nucleus by attaching to define recognition sequences termed “Nuclear Localization Sequences”. Importin-β as a segment of heterodimer connects with the pore complex, whereas Importin-α functions as a protein adaptor to attach the NLS to the cargo site. The fundamental ground of the Kapβ1 structure is 18 to 20 tandem HEAT motif repeats. In order to transfer “cargo into the nucleus”, Kapβ1 should connect with the “Nuclear Pore Complexes”. The study aims to assess the function of Kapβ1 impotent protein in nuclear transport. FG NUP purification, SPR measurements, MST, Kapα, and Kapβ1 purification have been used here to analyze the entire process. The process of nuclear transport comprises cargo bindings, cargo release, and cargo transport. It has been observed that the HEAT motifs attached to Kapβ1 at the schematic hydrophobic pocket on the protein surface.

Keyword : Cargo Bindings, FG Nups, Kapα, Kapβ1, NLSs, NPC, and Ran.