A Structural Basis for IκB Kinase 2 Activation Via Oligomerization-Dependent Trans Auto-Phosphorylation

@inproceedings{Polley2013ASB,
  title={A Structural Basis for IκB Kinase 2 Activation Via Oligomerization-Dependent Trans Auto-Phosphorylation},
  author={Smarajit Polley and D Huang and Arthur V. Hauenstein and Amanda J. Fusco and Xiangyang Zhong and Don Vu and B{\"a}rbel Schr{\"o}felbauer and Youngchang Kim and Alexander Hoffmann and Inder M Verma and Gourisankar Ghosh and T. J. Huxford},
  booktitle={PLoS biology},
  year={2013}
}
Activation of the IκB kinase (IKK) is central to NF-κB signaling. However, the precise activation mechanism by which catalytic IKK subunits gain the ability to induce NF-κB transcriptional activity is not well understood. Here we report a 4 Å x-ray crystal structure of human IKK2 (hIKK2) in its catalytically active conformation. The hIKK2 domain architecture closely resembles that of Xenopus IKK2 (xIKK2). However, whereas inactivated xIKK2 displays a closed dimeric structure, hIKK2 dimers adopt… CONTINUE READING

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Crystal structure of inhibitor of k B kinase b

  • G Xu, YC Lo, Q Li, G Napolitano, X Wu
  • Nature
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