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-Structure paper
| タイトル | Structure and mechanism of the HECT ligase HECTD3. |
|---|---|
| ジャーナル・号・ページ | Nat Commun, Vol. 17, Issue 1, Year 2026 |
| 掲載日 | 2026年2月14日 |
著者 | Jessica Huber / Diego Esposito / Sarah Maslen / Dominic O Chambers / J Mark Skehel / Katrin Rittinger / ![]() |
| PubMed 要旨 | HECT E3 ligases regulate many cellular processes, yet how they recognise their substrates and synthesise specific types of poly-ubiquitin chains is still incompletely understood. HECTD3, a member of ...HECT E3 ligases regulate many cellular processes, yet how they recognise their substrates and synthesise specific types of poly-ubiquitin chains is still incompletely understood. HECTD3, a member of the "other HECT" family, is implicated in the regulation of inflammation, apoptosis, and infection and highly expressed in several cancers. These functions are largely attributed to its ligase activity and modification of diverse substrates with different types of ubiquitin chains. We present a detailed analysis of the ligase activity of HECTD3, including its ubiquitin linkage preferences, oligomeric state and substrate ubiquitination. Using cryo-EM, we provide the full-length structures of HECTD3 in both apo and ubiquitin-loaded forms, revealing key insights into its domain organisation, including discovery of a distinct fold of the N-terminal region, and mechanistic features. Some of these are shared with other HECT ligases, while others are unique to HECTD3 and contribute to differences in its catalytic mechanisms and functional diversity. |
リンク | Nat Commun / PubMed:41690955 / PubMed Central |
| 手法 | EM (単粒子) / X線回折 |
| 解像度 | 1.61 - 6.38 Å |
| 構造データ | EMDB-53804, PDB-9r85: EMDB-53836, PDB-9r8t: EMDB-53852, PDB-9r94: ![]() PDB-9r6v: |
| 化合物 | ![]() ChemComp-MG: ![]() ChemComp-HOH: ![]() ChemComp-AYE: |
| 由来 |
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キーワード | LIGASE / E3-ligase / ubiquitin / ubiquitination / HECT-ligase |
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