1NFI

I-KAPPA-B-ALPHA/NF-KAPPA-B COMPLEX

1NFI の概要

• エントリーDOI: 10.2210/pdb1nfi/pdb
• 分子名称: NF-KAPPA-B P65, NF-KAPPA-B P50, I-KAPPA-B-ALPHA, ... (4 entities in total)
• 機能のキーワード: complex (transcription regulation-ank repeat), ankyrin repeat, complex (transcription reg-ank repeat) complex, complex (transcription reg/ank repeat)
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: Q04206 P19838; Cytoplasm: P25963
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 140603.66

構造登録者

Jacobs, M.D.,Harrison, S.C. (登録日: 1998-08-25, 公開日: 1998-11-18, 最終更新日: 2024-02-14)

主引用文献

Jacobs, M.D.,Harrison, S.C.
Structure of an IkappaBalpha/NF-kappaB complex.
Cell(Cambridge,Mass.), 95:749-758, 1998

PubMed Abstract: 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.

PubMed: 9865693
DOI: 10.1016/S0092-8674(00)81698-0

実験手法

X-RAY DIFFRACTION (2.7 Å)