Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structure and mechanism of the HECT ligase HECTD3.
Journal, issue, pages	Nat Commun, Year 2026
Publish date	Feb 14, 2026
Authors	Jessica Huber / Diego Esposito / Sarah Maslen / Dominic O Chambers / J Mark Skehel / Katrin Rittinger /
PubMed Abstract	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.
External links	Nat Commun / PubMed:41690955
Methods	EM (single particle) / X-ray diffraction
Resolution	1.61 - 6.38 Å
Structure data	53804 9r85 EMDB-53804, PDB-9r85: Cryo-EM structure of the E3 ligase HECTD3 conjugated to ubiquitin Method: EM (single particle) / Resolution: 3.04 Å 53836 9r8t EMDB-53836, PDB-9r8t: Cryo-EM structure of the E3 ligase HECTD3 Method: EM (single particle) / Resolution: 6.06 Å 53852 9r94 EMDB-53852, PDB-9r94: Cryo-EM structure of the E3 ligase HECTD3 Method: EM (single particle) / Resolution: 6.38 Å PDB-9r6v: Crystal structure of the DOC domain of the E3 ligase HECTD3 Method: X-RAY DIFFRACTION / Resolution: 1.61 Å
Chemicals	ChemComp-MG: Unknown entry ChemComp-HOH: WATER ChemComp-AYE: prop-2-en-1-amine
Source	homo sapiens (human)
Keywords	LIGASE / E3-ligase / ubiquitin / ubiquitination / HECT-ligase