SOX2 is important for self-renewal of undifferentiated embryonic stem-cells and maintaining the undifferentiated state of embryonic stem cells through interaction with other cellular factors, and is part of the Sex Determining Region Y (SRY) family which is involved in human sex determination. For the efficient and correct function of SOX2 it must be actively transported to the nucleus where it is able to bind DNA within the minor groove causing it to bend, causing transactivation by cooperative transcription factors such as Oct3/4. Nucleocytoplasmic transport processes have well characterised in literature; in the classical pathway nuclear cargo proteins are bound by importin alpha, which in turn are bound by importin beta to allow it to dock and be translocated through the nuclear pore complex. Here we describe the high resolution x-ray structure of Importin-alpha bound to the NLS region of SOX2, small angle x-ray scattering data, and functional data that describes its nuclear import. These findings provide an enhanced understanding of the mechanism by which SOX2 gains access to the nucleus, and in turn, knowledge of its cellular role in mediating stem cell differentiation.