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1nfi
From Proteopedia
I-KAPPA-B-ALPHA/NF-KAPPA-B COMPLEX
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.
Structure of an IkappaBalpha/NF-kappaB complex., Jacobs MD, Harrison SC, Cell. 1998 Dec 11;95(6):749-58. PMID:9865693
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1NFI is a 6 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Jacobs MD, Harrison SC. Structure of an IkappaBalpha/NF-kappaB complex. Cell. 1998 Dec 11;95(6):749-58. PMID:9865693
Page seeded by OCA on Wed Feb 18 05:08:30 2009

