1IKN

IKAPPABALPHA/NF-KAPPAB COMPLEX

Summary for 1IKN

• Entry DOI: 10.2210/pdb1ikn/pdb
• Descriptor: PROTEIN (NF-KAPPA-B P65 SUBUNIT), PROTEIN (NF-KAPPA-B P50D SUBUNIT), PROTEIN (I-KAPPA-B-ALPHA), ... (4 entities in total)
• Functional Keywords: transcription factor, ikb-nfkb complex
• Biological source: Mus musculus (house mouse); More
• Cellular location: Nucleus: Q04207; Nucleus. Isoform 5: Cytoplasm. Isoform 6: Nucleus. Isoform 7: Nucleus: P25799; Cytoplasm: P25963
• Total number of polymer chains: 3
• Total formula weight: 72766.02

Authors

Huxford, T.,Huang, D.-B.,Malek, S.,Ghosh, G. (deposition date: 1998-11-13, release date: 1999-04-12, Last modification date: 2023-08-16)

Primary citation

Huxford, T.,Huang, D.B.,Malek, S.,Ghosh, G.
The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation.
Cell(Cambridge,Mass.), 95:759-770, 1998

PubMed Abstract: IkappaBalpha regulates the transcription factor NF-kappaB through the formation of stable IkappaBalpha/NF-kappaB complexes. Prior to induction, IkappaBalpha retains NF-kappaB in the cytoplasm until the NF-kappaB activation signal is received. After activation, NF-kappaB is removed from gene promoters through association with nuclear IkappaBalpha, restoring the preinduction state. The 2.3 A crystal structure of IkappaBalpha in complex with the NF-kappaB p50/p65 heterodimer reveals mechanisms of these inhibitory activities. The presence of IkappaBalpha allows large en bloc movement of the NF-kappaB p65 subunit amino-terminal domain. This conformational change induces allosteric inhibition of NF-kappaB DNA binding. Amino acid residues immediately preceding the nuclear localization signals of both NF-kappaB p50 and p65 subunits are tethered to the IkappaBalpha amino-terminal ankyrin repeats, impeding NF-kappaB from nuclear import machinery recognition.

PubMed: 9865694
DOI: 10.1016/S0092-8674(00)81699-2

Experimental method

X-RAY DIFFRACTION (2.3 Å)