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...
Gespeichert in:
| Hauptverfasser: | , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
2016
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| In: |
Biochemical Society transactions
Year: 2016, Jahrgang: 44, Heft: 2, Pages: 613-618 |
| ISSN: | 1470-8752 |
| DOI: | 10.1042/BST20150283 |
| Online-Zugang: | 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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| Verfasserangaben: | Francesca Fanelli, Angelo Felline, Francesco Raimondi and Michele Seeber |
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| 520 | |a 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. | ||
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