The 1.6 angstroms resolution crystal structure of nuclear transport factor 2 (NTF2)

J Mol Biol. 1996 Jul 19;260(3):422-31. doi: 10.1006/jmbi.1996.0411.


Nuclear transport factor 2 (NTF2) facilitates protein transport into the nucleus and interacts with both the small Ras-like GTPase Ran and nucleoporin p62. We have determined the structure of bacterially expressed rat NTF2 at 1.6 angstroms resolution using X-ray crystallography. The NTF2 polypeptide chain forms an alpha + beta barrel that opens at one end to form a distinctive hydrophobic cavity and its fold is homologous to that of scytalone dehydratase. The NTF2 hydrophobic cavity is a candidate for a potential binding site for other proteins involved in nuclear import such as Ran and nucleoporin p62. In addition, the hydrophobic cavity contains a putative catalytic Asp-His pair, which raises the possibility of an unanticipated enzymatic activity of the molecule that may have implications for the molecular mechanism of nuclear protein import.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Carrier Proteins / chemistry*
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism
  • Crystallography, X-Ray
  • Gene Expression
  • Hydro-Lyases / chemistry
  • Membrane Glycoproteins / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Pore Complex Proteins
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism
  • Nucleocytoplasmic Transport Proteins*
  • Protein Binding
  • Protein Conformation
  • Protein Folding
  • Rats
  • Sequence Homology, Amino Acid
  • ran GTP-Binding Protein


  • Carrier Proteins
  • Membrane Glycoproteins
  • Nuclear Pore Complex Proteins
  • Nuclear Proteins
  • Nucleocytoplasmic Transport Proteins
  • Nutf2 protein, rat
  • nuclear pore protein p62
  • ran GTP-Binding Protein
  • Hydro-Lyases
  • scytalone dehydratase