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

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: 10201409
DOI: 10.1038/7625

Experimental method

X-RAY DIFFRACTION (2.5 Å)