1H, 13C, and 15N resonance assignments of the C-terminal lobe of the human HECT E3 ubiquitin ligase ITCH

ITCH ( aka Atrophin-1-interacting protein 4) is a prominent member of the NEDD4 HECT ( H omologous to E 6AP C-T erminus) E3 ubiquitin ligase family that regulates numerous cellular functions including inflammatory responses through T-cell activation, cell differentiation, and apoptosis. Known intrac...

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Bibliographic Details
Published in:Biomolecular NMR assignments 2019-04, Vol.13 (1), p.15-20
Main Authors: Beasley, Steven A., Bardhi, Roela, Spratt, Donald E.
Format: Article
Language:English
Subjects:
Apoptosis
Biochemistry
Biological and Medical Physics
Biophysics
C-Terminus
Cell activation
Cell differentiation
Inflammation
Intracellular signalling
Lymphocytes T
Magnetic resonance spectroscopy
NMR
Nuclear magnetic resonance
Physics
Physics and Astronomy
Polymer Sciences
Protein structure
Proteins
Resonance
Transcription factors
Ubiquitin
Ubiquitin-protein ligase
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Summary:ITCH ( aka Atrophin-1-interacting protein 4) is a prominent member of the NEDD4 HECT ( H omologous to E 6AP C-T erminus) E3 ubiquitin ligase family that regulates numerous cellular functions including inflammatory responses through T-cell activation, cell differentiation, and apoptosis. Known intracellular targets of ITCH-dependent ubiquitylation include receptor proteins, signaling molecules, and transcription factors. The HECT C -terminal lobe of ITCH contains the conserved catalytic cysteine required for the covalent attachment of ubiquitin onto a substrate and polyubiquitin chain assembly. We report here the complete experimentally determined 1 H, 13 C, and 15 N backbone and sidechain resonance assignments for the HECT C -terminal lobe of ITCH (residues 784–903) using heteronuclear, multidimensional NMR spectroscopy. These resonance assignments will be used in future NMR-based studies to examine the role of dynamics and conformational flexibility in HECT-dependent ubiquitylation as well as deciphering the structural and biochemical basis for polyubiquitin chain synthesis and specificity by ITCH.
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-018-9843-2