Nuclear transport: randy couples.
The recently solved structures of the Ran GTPase with a Ran-binding domain and with karyopherin-beta2 have revealed unusually tight embraces that provide important insights into the mechanism of nuclear transport and the many ways in which common protein folds are adapted to perform very different functions.
Macara
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Department of Pharmacology, Center for Cell Signaling, University of Virginia, 7196 Hospital West, 577, Health Sciences Center, Charlottesville, Virginia 22908, USA. imacara@virginia.edu
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D001693:Biological Transport, Active; D002467:Cell Nucleus / Q000378:metabolism*; D020558:GTP Phosphohydrolases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D028884:Karyopherins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011487:Protein Conformation; D018160:Receptors, Cytoplasmic and Nuclear / Q000737:chemistry / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D020931:ran GTP-Binding Protein
D028884:Karyopherins; D009687:Nuclear Proteins; D018160:Receptors, Cytoplasmic and Nuclear; D020558:GTP Phosphohydrolases; D020931:ran GTP-Binding Protein