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Active State-like Conformational Elements in the β(2)-AR and a Photoactivated Intermediate of Rhodopsin Identified by Dynamic Properties of GPCRs†

[Image: see text] G-Protein-coupled receptors (GPCRs) adopt various functionally relevant conformational states in cell signaling processes. Recently determined crystal structures of rhodopsin and the β(2)-adrenergic receptor (β(2)-AR) offer insight into previously uncharacterized active conformatio...

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Detalles Bibliográficos
Autores principales: Han, Daniel S., Wang, Simon X., Weinstein, Harel
Formato: Texto
Lenguaje:English
Publicado: American Chemical Society 2008
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2664832/
https://www.ncbi.nlm.nih.gov/pubmed/18558776
http://dx.doi.org/10.1021/bi800442g
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author Han, Daniel S.
Wang, Simon X.
Weinstein, Harel
author_facet Han, Daniel S.
Wang, Simon X.
Weinstein, Harel
author_sort Han, Daniel S.
collection PubMed
description [Image: see text] G-Protein-coupled receptors (GPCRs) adopt various functionally relevant conformational states in cell signaling processes. Recently determined crystal structures of rhodopsin and the β(2)-adrenergic receptor (β(2)-AR) offer insight into previously uncharacterized active conformations, but the molecular states of these GPCRs are likely to contain both inactive and active-like conformational elements. We have identified conformational rearrangements in the dynamics of the TM7−HX8 segment that relate to the properties of the conserved NPxxY(x)5,6F motif and show that they can be used to identify active state-like conformational elements in the corresponding regions of the new structures of rhodopsin and the β(2)-AR.
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spelling pubmed-26648322009-04-06 Active State-like Conformational Elements in the β(2)-AR and a Photoactivated Intermediate of Rhodopsin Identified by Dynamic Properties of GPCRs† Han, Daniel S. Wang, Simon X. Weinstein, Harel Biochemistry [Image: see text] G-Protein-coupled receptors (GPCRs) adopt various functionally relevant conformational states in cell signaling processes. Recently determined crystal structures of rhodopsin and the β(2)-adrenergic receptor (β(2)-AR) offer insight into previously uncharacterized active conformations, but the molecular states of these GPCRs are likely to contain both inactive and active-like conformational elements. We have identified conformational rearrangements in the dynamics of the TM7−HX8 segment that relate to the properties of the conserved NPxxY(x)5,6F motif and show that they can be used to identify active state-like conformational elements in the corresponding regions of the new structures of rhodopsin and the β(2)-AR. American Chemical Society 2008-06-18 2008-07-15 /pmc/articles/PMC2664832/ /pubmed/18558776 http://dx.doi.org/10.1021/bi800442g Text en Copyright © 2008 American Chemical Society http://pubs.acs.org This is an open-access article distributed under the ACS AuthorChoice Terms & Conditions. Any use of this article, must conform to the terms of that license which are available at http://pubs.acs.org. 40.75
spellingShingle Han, Daniel S.
Wang, Simon X.
Weinstein, Harel
Active State-like Conformational Elements in the β(2)-AR and a Photoactivated Intermediate of Rhodopsin Identified by Dynamic Properties of GPCRs†
title Active State-like Conformational Elements in the β(2)-AR and a Photoactivated Intermediate of Rhodopsin Identified by Dynamic Properties of GPCRs†
title_full Active State-like Conformational Elements in the β(2)-AR and a Photoactivated Intermediate of Rhodopsin Identified by Dynamic Properties of GPCRs†
title_fullStr Active State-like Conformational Elements in the β(2)-AR and a Photoactivated Intermediate of Rhodopsin Identified by Dynamic Properties of GPCRs†
title_full_unstemmed Active State-like Conformational Elements in the β(2)-AR and a Photoactivated Intermediate of Rhodopsin Identified by Dynamic Properties of GPCRs†
title_short Active State-like Conformational Elements in the β(2)-AR and a Photoactivated Intermediate of Rhodopsin Identified by Dynamic Properties of GPCRs†
title_sort active state-like conformational elements in the β(2)-ar and a photoactivated intermediate of rhodopsin identified by dynamic properties of gpcrs†
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2664832/
https://www.ncbi.nlm.nih.gov/pubmed/18558776
http://dx.doi.org/10.1021/bi800442g
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