3QA8

Crystal Structure of inhibitor of kappa B kinase beta

3QA8 の概要

• エントリーDOI: 10.2210/pdb3qa8/pdb
• 関連するPDBエントリー: 3QAD
• 分子名称: MGC80376 protein (1 entity in total)
• 機能のキーワード: kinase ubiquitin-like domain, phosphorylation, kinase domain, ubiquitin-like domain, kinase, substrate binding, immune system, signaling protein
• 由来する生物種: Xenopus laevis (clawed frog,common platanna,platanna)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 622987.06

構造登録者

Xu, G.,Lo, Y.C.,Li, Q.,Napolitano, G.,Wu, X.,Jiang, X.,Dreano, M.,Karin, M.,Wu, H. (登録日: 2011-01-10, 公開日: 2011-04-06, 最終更新日: 2024-05-22)

主引用文献

Xu, G.,Lo, Y.C.,Li, Q.,Napolitano, G.,Wu, X.,Jiang, X.,Dreano, M.,Karin, M.,Wu, H.
Crystal structure of inhibitor of kappa B kinase beta.
Nature, 472:325-330, 2011

PubMed Abstract: Inhibitor of κB (IκB) kinase (IKK) phosphorylates IκB proteins, leading to their degradation and the liberation of nuclear factor κB for gene transcription. Here we report the crystal structure of IKKβ in complex with an inhibitor, at a resolution of 3.6 Å. The structure reveals a trimodular architecture comprising the kinase domain, a ubiquitin-like domain (ULD) and an elongated, α-helical scaffold/dimerization domain (SDD). Unexpectedly, the predicted leucine zipper and helix-loop-helix motifs do not form these structures but are part of the SDD. The ULD and SDD mediate a critical interaction with IκBα that restricts substrate specificity, and the ULD is also required for catalytic activity. The SDD mediates IKKβ dimerization, but dimerization per se is not important for maintaining IKKβ activity and instead is required for IKKβ activation. Other IKK family members, IKKα, TBK1 and IKK-i, may have a similar trimodular architecture and function.

PubMed: 21423167
DOI: 10.1038/nature09853

実験手法

X-RAY DIFFRACTION (3.6 Å)