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2 楼
吴号Michael Karin强强联手
搞结构灌水灌的真快
Crystal structure of inhibitor of κB kinase β
Guozhou Xu, Yu-Chih Lo, Qiubai Li, Gennaro Napolitano, Xuefeng Wu, Xuliang Jiang, Michel Dreano,
Michael Karin & Hao Wu
Department of Biochemistry, Weill Cornell Medical College, New York, New York 10021, USA
Guozhou Xu, Yu-Chih Lo, Qiubai Li & Hao Wu
Department of Pharmacology, University of California at San Diego, La Jolla, California 92093, USA
Gennaro Napolitano, Xuefeng Wu & Michael Karin
Nature (2011) doi:10.1038/nature09853
Received 27 September 2010 Accepted 17 January 2011 Published online 20 March 2011
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.
搞结构灌水灌的真快
Crystal structure of inhibitor of κB kinase β
Guozhou Xu, Yu-Chih Lo, Qiubai Li, Gennaro Napolitano, Xuefeng Wu, Xuliang Jiang, Michel Dreano,
Michael Karin & Hao Wu
Department of Biochemistry, Weill Cornell Medical College, New York, New York 10021, USA
Guozhou Xu, Yu-Chih Lo, Qiubai Li & Hao Wu
Department of Pharmacology, University of California at San Diego, La Jolla, California 92093, USA
Gennaro Napolitano, Xuefeng Wu & Michael Karin
Nature (2011) doi:10.1038/nature09853
Received 27 September 2010 Accepted 17 January 2011 Published online 20 March 2011
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.
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