1F59
IMPORTIN-BETA-FXFG NUCLEOPORIN COMPLEX
Summary for 1F59
Entry DOI | 10.2210/pdb1f59/pdb |
Descriptor | IMPORTIN BETA-1, FXFG NUCLEOPORIN REPEATS (2 entities in total) |
Functional Keywords | protein-protein complex, transport protein receptor |
Biological source | Homo sapiens (human) More |
Cellular location | Cytoplasm : Q14974 |
Total number of polymer chains | 4 |
Total formula weight | 104144.48 |
Authors | Bayliss, R.,Littlewood, T.,Stewart, M. (deposition date: 2000-06-13, release date: 2000-08-16, Last modification date: 2024-02-07) |
Primary citation | Bayliss, R.,Littlewood, T.,Stewart, M. Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking. Cell(Cambridge,Mass.), 102:99-108, 2000 Cited by PubMed Abstract: We describe the crystal structure of a complex between importin-beta residues 1-442 (Ib442) and five FxFG nucleoporin repeats from Nsp1p. Nucleoporin FxFG cores bind on the convex face of Ib442 to a primary site between the A helices of HEAT repeats 5 and 6, and to a secondary site between HEAT repeats 6 and 7. Mutations at importin-beta Ile178 in the primary FxFG binding site reduce both binding and nuclear protein import, providing direct evidence for the functional significance of the importin-beta-FxFG interaction. The FxFG binding sites on importin-beta do not overlap with the RanGTP binding site. Instead, RanGTP may release importin-beta from FxFG nucleoporins by generating a conformational change that alters the structure of the FxFG binding site. PubMed: 10929717DOI: 10.1016/S0092-8674(00)00014-3 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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