The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation.
Copyright policy The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation.
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.
- University of California, San Diego United States
Protein Conformation, Molecular Sequence Data, Nuclear Localization Signals, NF-kappa B, Transcription Factor RelA, NF-kappa B p50 Subunit, DNA, Crystallography, X-Ray, DNA-Binding Proteins, NF-KappaB Inhibitor alpha, I-kappa B Proteins, Amino Acid Sequence, Peptides, Dimerization
Protein Conformation, Molecular Sequence Data, Nuclear Localization Signals, NF-kappa B, Transcription Factor RelA, NF-kappa B p50 Subunit, DNA, Crystallography, X-Ray, DNA-Binding Proteins, NF-KappaB Inhibitor alpha, I-kappa B Proteins, Amino Acid Sequence, Peptides, Dimerization
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