Characterisation of HOIP RBR E3 ligase conformational dynamics using integrative modelling.


Journal

Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288

Informations de publication

Date de publication:
08 09 2022
Historique:
received: 21 05 2022
accepted: 22 08 2022
entrez: 8 9 2022
pubmed: 9 9 2022
medline: 14 9 2022
Statut: epublish

Résumé

Multidomain proteins composed of individual domains connected by flexible linkers pose a challenge for structural studies due to their intrinsic conformational dynamics. Integrated modelling approaches provide a means to characterise protein flexibility by combining experimental measurements with molecular simulations. In this study, we characterise the conformational dynamics of the catalytic RBR domain of the E3 ubiquitin ligase HOIP, which regulates immune and inflammatory signalling pathways. Specifically, we combine small angle X-ray scattering experiments and molecular dynamics simulations to generate weighted conformational ensembles of the HOIP RBR domain using two different approaches based on maximum parsimony and maximum entropy principles. Both methods provide optimised ensembles that are instrumental in rationalising observed differences between SAXS-based solution studies and available crystal structures and highlight the importance of interdomain linker flexibility.

Identifiants

pubmed: 36076045
doi: 10.1038/s41598-022-18890-6
pii: 10.1038/s41598-022-18890-6
pmc: PMC9458678
doi:

Substances chimiques

Proteins 0
Ubiquitin-Protein Ligases EC 2.3.2.27

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

15201

Subventions

Organisme : Wellcome Trust
ID : FC001142
Pays : United Kingdom
Organisme : Medical Research Council
ID : FC001142
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/T002212/1
Pays : United Kingdom
Organisme : Cancer Research UK
ID : FC001142
Pays : United Kingdom

Informations de copyright

© 2022. The Author(s).

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Auteurs

Marius Kausas (M)

New Hunt's House, King's College London, Guy's Campus, London, SE1 1UL, UK.
Molecular Structure of Cell Signalling Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.
Illumina Centre, 19 Granta Park, Great Abington, Cambridge, CB21 6DF, Cambridgeshire, UK.

Diego Esposito (D)

Molecular Structure of Cell Signalling Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK.

Katrin Rittinger (K)

Molecular Structure of Cell Signalling Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK. katrin.rittinger@crick.ac.uk.

Franca Fraternali (F)

New Hunt's House, King's College London, Guy's Campus, London, SE1 1UL, UK. franca.fraternali@kcl.ac.uk.
The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK. franca.fraternali@kcl.ac.uk.

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Classifications MeSH