Small GTPase Ran: Depicting the nucleotide-specific conformational landscape of the functionally important C-terminus.

ABSTRACT: The small GTPase Ran is the main regulator of the nucleo-cytoplasmic import and export through the nuclear pore complex. It functions as a molecular switch cycling between the GDP-bound inactive and GTP-bound active state. It consists of a globular (G) domain and a C-terminal region, which is bound to the G-domain in the inactive, GDP-bound states. Crystal structures of the GTP-bound active form complexed with Ran binding proteins (RanBP) show that the C-terminus undergoes a large conformational change, embracing Ran binding domains (RanBD). Whereas in the crystal structures of macromolecular complexes not containing RanBDs the structure of the C-terminal segment remains unresolved, indicating its large conformational flexibility. This movement could not have been followed either by experi

SUBMITTER: Czigleczki J 

PROVIDER: S-EPMC9885160 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature