Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport

Article Abstract:

The crystal structure of the complex of the first Ran-binding domain of human Ran-binding protein 2 (RanBP2) with Ran bound to a non-hydrolysable GTP analogue indicates a molecular mechanism to explain the function of RanBPs in nuclear transport. It is likely that the main function of Ran-binding domains is to sequester the C-terminal extension of Ran. There is currently no structural model for Ran-transport-factor complexes, and this makes it hard to identify the function of RanBPs as a 'dissociator' of nuclear-export complexes.

Carrier proteins, Transport proteins, Cell cycle

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Structural insight into filament formation by mammalian septins

Article Abstract:

The structures of the human SEPT2 G domain and the heterotrimeric human SEPT2-SEPT6-SEPT7 complex are presented. A universal bipolar polymer building block is revealed by these structures.

Composition, G proteins, Report

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The GTPase-activating protein Rap1GAP uses a catalytic asparagine

Article Abstract:

Rap1GAP provides a catalytic asparagine to stimulate GTP hydrolysis is demonstrated. Implications for the disease tuberous sclerosis are discussed.

United States, Influence, Enzymes, Hydrolases, Guanosine triphosphatase, GTPases, Asparagine

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