Structure network analysis to gain insights into GPCR function

G protein coupled receptors (GPCRs) are allosteric proteins whose functioning fundamentals are the communication between the two poles of the helix bundle. Protein structure network (PSN) analysis is one of the graph theory-based approaches currently used to investigate the structural communication...

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Bibliographic Details
Main Authors: Fanelli, Francesca (Author) , Felline, Angelo (Author) , Raimondi, Francesco (Author) , Seeber, Michele (Author)
Format: Article (Journal)
Language:English
Published: 2016
In: Biochemical Society transactions
Year: 2016, Volume: 44, Issue: 2, Pages: 613-618
ISSN:1470-8752
DOI:10.1042/BST20150283
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1042/BST20150283
Verlag, lizenzpflichtig, Volltext: /biochemsoctrans/article/44/2/613/67512/Structure-network-analysis-to-gain-insights-into
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Author Notes:Francesca Fanelli, Angelo Felline, Francesco Raimondi and Michele Seeber
Description
Summary:G protein coupled receptors (GPCRs) are allosteric proteins whose functioning fundamentals are the communication between the two poles of the helix bundle. Protein structure network (PSN) analysis is one of the graph theory-based approaches currently used to investigate the structural communication in biomolecular systems. Information on system's dynamics can be provided by atomistic molecular dynamics (MD) simulations or coarse grained elastic network models paired with normal mode analysis (ENM-NMA). The present review article describes the application of PSN analysis to uncover the structural communication in G protein coupled receptors (GPCRs). Strategies to highlight changes in structural communication upon misfolding, dimerization and activation are described. Focus is put on the ENM-NMA-based strategy applied to the crystallographic structures of rhodopsin in its inactive (dark) and signalling active (meta II (MII)) states, highlighting changes in structure network and centrality of the retinal chromophore in differentiating the inactive and active states of the receptor.
Item Description:Gesehen am 19.06.2020
Physical Description:Online Resource
ISSN:1470-8752
DOI:10.1042/BST20150283