1IAL
IMPORTIN ALPHA, MOUSE
Summary for 1IAL
| Entry DOI | 10.2210/pdb1ial/pdb |
| Descriptor | IMPORTIN ALPHA (2 entities in total) |
| Functional Keywords | nuclear import receptor, nuclear localization signal, armadillo repeats, autoinhibition, intrasteric regulation |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 49333.24 |
| Authors | Kobe, B. (deposition date: 1999-01-12, release date: 1999-06-15, Last modification date: 2024-05-22) |
| Primary citation | Kobe, B. Autoinhibition by an internal nuclear localization signal revealed by the crystal structure of mammalian importin alpha. Nat.Struct.Biol., 6:388-397, 1999 Cited by PubMed Abstract: Importin alpha is the nuclear import receptor that recognizes classical monopartite and bipartite nuclear localization signals (NLSs). The structure of mouse importin alpha has been determined at 2.5 A resolution. The structure shows a large C-terminal domain containing armadillo repeats, and a less structured N-terminal importin beta-binding domain containing an internal NLS bound to the NLS-binding site. The structure explains the regulatory switch between the cytoplasmic, high-affinity form, and the nuclear, low-affinity form for NLS binding of the nuclear import receptor predicted by the current models of nuclear import. Importin beta conceivably converts the low- to high-affinity form by binding to a site overlapping the autoinhibitory sequence. The structure also has implications for understanding NLS recognition, and the structures of armadillo and HEAT repeats. PubMed: 10201409DOI: 10.1038/7625 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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