Structural dynamics of ABC transporters: molecular simulation studies.
ABC transporter
ATP binding and hydrolysis
allosteric communication
conformational transition
coupling helix
substrate
Journal
Biochemical Society transactions
ISSN: 1470-8752
Titre abrégé: Biochem Soc Trans
Pays: England
ID NLM: 7506897
Informations de publication
Date de publication:
26 02 2021
26 02 2021
Historique:
received:
20
11
2020
revised:
02
02
2021
accepted:
03
02
2021
pubmed:
27
2
2021
medline:
27
1
2022
entrez:
26
2
2021
Statut:
ppublish
Résumé
The biological activities of living organisms involve various inputs and outputs. The ATP-driven substances (biomolecules) responsible for these kinds of activities through membrane (i.e. uptake and efflux of substrates) include ATP-binding cassette (ABC) transporters, some of which play important roles in multidrug resistance. The basic architecture of ABC transporters comprises transmembrane domains (TMDs) and nucleotide-binding domains (NBDs). The functional dynamics (substrate transport) of ABC transporters are realized by concerted motions, such as NBD dimerization, mechanical transmission via coupling helices (CHs), and the translocation of substrates through TMDs, which are induced by the binding and/or hydrolysis of ATP molecules and substrates. In this mini-review, we briefly discuss recent progresses in the structural dynamics as revealed by molecular simulation studies at all-atom (AA), coarse-grained (CG), and quantum mechanics/molecular mechanics (QM/MM) levels.
Identifiants
pubmed: 33634827
pii: 227946
doi: 10.1042/BST20200710
doi:
Substances chimiques
ATP-Binding Cassette Transporters
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
405-414Informations de copyright
© 2021 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.