The 1.6 angstroms resolution crystal structure of nuclear transport factor 2 (NTF2).
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.
Mesh Terms:
Amino Acid Sequence, Animals, Carrier Proteins, Crystallography, X-Ray, Gene Expression, Hydro-Lyases, Membrane Glycoproteins, Models, Molecular, Molecular Sequence Data, Nuclear Proteins, Nucleocytoplasmic Transport Proteins, Protein Binding, Protein Conformation, Protein Folding, Rats, Sequence Homology, Amino Acid, ran GTP-Binding Protein
Amino Acid Sequence, Animals, Carrier Proteins, Crystallography, X-Ray, Gene Expression, Hydro-Lyases, Membrane Glycoproteins, Models, Molecular, Molecular Sequence Data, Nuclear Proteins, Nucleocytoplasmic Transport Proteins, Protein Binding, Protein Conformation, Protein Folding, Rats, Sequence Homology, Amino Acid, ran GTP-Binding Protein
J. Mol. Biol.
Date: Jul. 19, 1996
PubMed ID: 8757804
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