Cation-π Interactions and their Functional Roles in Membrane Proteins.


Journal

Journal of molecular biology
ISSN: 1089-8638
Titre abrégé: J Mol Biol
Pays: Netherlands
ID NLM: 2985088R

Informations de publication

Date de publication:
20 08 2021
Historique:
received: 18 03 2021
revised: 27 04 2021
accepted: 27 04 2021
pubmed: 7 5 2021
medline: 21 10 2021
entrez: 6 5 2021
Statut: ppublish

Résumé

Cation-π interactions arise as a result of strong attractive forces between positively charged entities and the π-electron cloud of aromatic groups. The physicochemical characteristics of cation-π interactions are particularly well-suited to the dual hydrophobic/hydrophilic environment of membrane proteins. As high-resolution structural data of membrane proteins bring molecular features into increasingly sharper view, cation-π interactions are gaining traction as essential contributors to membrane protein chemistry, function, and pharmacology. Here we review the physicochemical properties of cation-π interactions and present several prominent examples which demonstrate significant roles for this specialized biological chemistry.

Identifiants

pubmed: 33957146
pii: S0022-2836(21)00249-7
doi: 10.1016/j.jmb.2021.167035
pmc: PMC8338773
mid: NIHMS1702731
pii:
doi:

Substances chimiques

Cations 0
Membrane Proteins 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

167035

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM122420
Pays : United States
Organisme : NHLBI NIH HHS
ID : F32 HL149184
Pays : United States
Organisme : NIGMS NIH HHS
ID : P41 GM104601
Pays : United States
Organisme : NINDS NIH HHS
ID : R24 NS104617
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM106569
Pays : United States

Informations de copyright

Copyright © 2021. Published by Elsevier Ltd.

Déclaration de conflit d'intérêts

Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

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Auteurs

Daniel T Infield (DT)

Department of Molecular Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, IA 52246, USA.

Ali Rasouli (A)

Theoretical and Computational Biophysics Group, NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA; Department of Biochemistry, and Center for Biophysics and Quantitative Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.

Grace D Galles (GD)

Department of Molecular Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, IA 52246, USA; Unnatural Protein Facility, Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331, USA.

Christophe Chipot (C)

Theoretical and Computational Biophysics Group, NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA; Laboratoire International Associé CNRS-University of Illinois, Unité mixte de recherche n°70a9, Université de Lorraine, France; Department of Physics, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.

Emad Tajkhorshid (E)

Theoretical and Computational Biophysics Group, NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA; Department of Biochemistry, and Center for Biophysics and Quantitative Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.

Christopher A Ahern (CA)

Department of Molecular Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, IA 52246, USA.

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