抄録
HOIL-1L and its binding partner HOIP are essential components of the E3-ligase complex that generates linear ubiquitin (Ub) chains, which are critical regulators of NF-κB activation. Using crystallographic and mutational approaches, we characterize the unexpected structural basis for the specific interaction between the Ub-like domain (UBL) of HOIL-1L and the Ub-associated domain (UBA) of HOIP. Our data indicate the functional significance of this non-canonical mode of UBA-UBL interaction in E3 complex formation and subsequent NF-κB activation. This study highlights the versatility and specificity of proteing-protein interactions involving Ub/UBLs and their cognate proteins.
本文言語 | English |
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ページ(範囲) | 462-468 |
ページ数 | 7 |
ジャーナル | EMBO Reports |
巻 | 13 |
号 | 5 |
DOI | |
出版ステータス | Published - 2012 5 1 |
外部発表 | はい |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Genetics