A glimpse into the molecular mechanism of integral membrane proteins through hydrogen-deuterium exchange mass spectrometry.
GPCRs
allosteric coupling
conformational dynamics
hydrogen-deuterium exchange mass spectrometry
integral membrane proteins
transporters
Journal
Protein science : a publication of the Protein Society
ISSN: 1469-896X
Titre abrégé: Protein Sci
Pays: United States
ID NLM: 9211750
Informations de publication
Date de publication:
06 2020
06 2020
Historique:
received:
28
02
2020
revised:
11
03
2020
accepted:
11
03
2020
pubmed:
15
3
2020
medline:
24
2
2021
entrez:
15
3
2020
Statut:
ppublish
Résumé
Integral membrane proteins (IMPs) control countless fundamental biological processes and constitute the majority of drug targets. For this reason, uncovering their molecular mechanism of action has long been an intense field of research. They are, however, notoriously difficult to work with, mainly due to their localization within the heterogeneous of environment of the biological membrane and the instability once extracted from the lipid bilayer. High-resolution structures have unveiled many mechanistic aspects of IMPs but also revealed that the elucidation of static pictures has limitations. Hydrogen-deuterium exchange coupled to mass spectrometry (HDX-MS) has recently emerged as a powerful biophysical tool for interrogating the conformational dynamics of proteins and their interactions with ligands. Its versatility has proven particularly useful to reveal mechanistic aspects of challenging classes of proteins such as IMPs. This review recapitulates the accomplishments of HDX-MS as it has matured into an essential tool for membrane protein structural biologists.
Identifiants
pubmed: 32170968
doi: 10.1002/pro.3853
pmc: PMC7255514
doi:
Substances chimiques
Lipid Bilayers
0
Membrane Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
1285-1301Informations de copyright
© 2020 The Authors. Protein Science published by Wiley Periodicals, Inc. on behalf of The Protein Society.
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