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Atomic resolution structures in nuclear transport.

Katherine E Süel1, Ahmet E Cansizoglu, Yuh Min Chook

  • 1Department of Pharmacology, University of Texas Southwestern Medical Center at Dallas, 6001 Forest Park, Dallas, TX 75390-9041, USA.

Methods (San Diego, Calif.)
|August 30, 2006
PubMed
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This paper catalogs 53 atomic resolution structures of nuclear transport proteins. These structures offer valuable insights for biochemical and cell biological studies, aiding protein analysis and manipulation.

Area of Science:

  • Structural Biology
  • Molecular Biology
  • Cell Biology

Background:

  • Nuclear transport is crucial for cellular function, involving numerous protein components.
  • Atomic resolution structures are essential for understanding molecular mechanisms.
  • The Protein Data Bank (PDB) houses structural data for biological molecules.

Purpose of the Study:

  • To catalog existing atomic resolution structures of nuclear transport proteins.
  • To provide a resource for researchers studying nuclear transport.
  • To guide mutagenesis and overexpression of recombinant nuclear transport proteins.

Main Methods:

  • Literature search and data compilation from the Protein Data Bank (PDB).
  • Inclusion of both crystal and Nuclear Magnetic Resonance (NMR) structures.

Related Experiment Videos

  • Focus on structures relevant to mutagenesis and recombinant protein studies.

    • Main Results:

    • A catalog of 53 distinct structures of nuclear transport protein components is presented.
    • These structures offer detailed insights into the molecular architecture of the nuclear transport machinery.
    • The catalog includes information pertinent to experimental manipulation of these proteins.

    Conclusions:

    • The availability of 53 structures significantly enhances the study of nuclear transport mechanisms.
    • This structural information serves as a foundation for future biochemical and cell biological investigations.
    • Researchers can leverage this catalog to facilitate protein engineering and functional studies.