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Article

DARPin-assisted crystallography of the CC2-LZ domain of NEMO reveals a coupling between dimerization and ubiquitin binding.

Journal of molecular biology - 8 Jan 2010

Grubisha Olivera, Kaminska Monika, Duquerroy Stéphane, Fontan Elisabeth, Cordier Florence, Haouz Ahmed, Raynal Bertrand, Chiaravalli Jeanne, Delepierre Muriel, Israël Alain, Véron Michel, Agou Fabrice

Abstract excerpt

NEMO is an integral part of the IkappaB kinase complex and serves as a molecular switch by which the NF-kappaB signaling pathway can be regulated. Oligomerization and polyubiquitin (poly-Ub) binding, mediated through the regulatory CC2-LZ domain, were shown to be key features governing NEMO function, but the relationship between these two activities remains unclear. In this study, we solved the structure of this...

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Identifiers

PMID: 19854204
DOI: 10.1016/j.jmb.2009.10.018

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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