1nfi
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(New page: 200px<br /> <applet load="1nfi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nfi, resolution 2.70Å" /> '''I-KAPPA-B-ALPHA/NF-...)
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Revision as of 16:14, 12 November 2007
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I-KAPPA-B-ALPHA/NF-KAPPA-B COMPLEX
Contents |
Overview
The inhibitory protein, IkappaBalpha, sequesters the transcription factor, NF-kappaB, as an inactive complex in the cytoplasm. The structure of the, IkappaBalpha ankyrin repeat domain, bound to a partially truncated, NF-kappaB heterodimer (p50/ p65), has been determined by X-ray, crystallography at 2.7 A resolution. It shows a stack of six IkappaBalpha, ankyrin repeats facing the C-terminal domains of the NF-kappaB Rel, homology regions. Contacts occur in discontinuous patches, suggesting a, combinatorial quality for ankyrin repeat specificity. The first two, repeats cover an alpha helically ordered segment containing the p65, nuclear localization signal. The position of the sixth ankyrin repeat, shows that full-length IkappaBalpha will occlude the NF-kappaB DNA-binding, cleft. The orientation of IkappaBalpha in the complex places its N- and, C-terminal regions in appropriate locations for their known regulatory, functions.
Disease
Known diseases associated with this structure: Ectodermal dysplasia, anhidrotic, with T-cell immunodeficiency OMIM:[164008]
About this Structure
1NFI is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of an IkappaBalpha/NF-kappaB complex., Jacobs MD, Harrison SC, Cell. 1998 Dec 11;95(6):749-58. PMID:9865693
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