The 1.6 Å 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 Å resolution using X-ray crystallography. The NTF2 polypeptide chain f...

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Bibliographic Details
Published in:Journal of molecular biology 1996-07, Vol.260 (3), p.422-431
Main Authors: Bullock, Timothy L., Clarkson, David W., Kent, Helen M., Stewart, Murray
Format: Article
Language:English
Subjects:
hydrophobic cavity
interactions
nuclear import
nucleoporin p62
Ran
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Summary: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 Å resolution using X-ray crystallography. The NTF2 polypeptide chain forms an α + β 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.
ISSN:0022-2836
1089-8638
DOI:10.1006/jmbi.1996.0411