1ikn
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(New page: 200px<br /> <applet load="1ikn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ikn, resolution 2.300Å" /> '''IKAPPABALPHA/NF-KA...)
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Revision as of 15:24, 12 November 2007
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IKAPPABALPHA/NF-KAPPAB COMPLEX
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Ectodermal dysplasia, anhidrotic, with T-cell immunodeficiency OMIM:[164008]
About this Structure
1IKN is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
Reference
The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation., Huxford T, Huang DB, Malek S, Ghosh G, Cell. 1998 Dec 11;95(6):759-70. PMID:9865694
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