dc.contributor.author
Krug, Ulrike
dc.contributor.author
Gloge, Anika
dc.contributor.author
Schmidt, Peter
dc.contributor.author
Becker-Baldus, Johanna
dc.contributor.author
Bernhard, Frank
dc.contributor.author
Kaiser, Anette
dc.contributor.author
Montag, Cindy
dc.contributor.author
Gauglitz, Marcel
dc.contributor.author
Vishnivetskiy, Sergey A.
dc.contributor.author
Gurevich, Vsevolod V.
dc.date.accessioned
2021-01-04T11:47:23Z
dc.date.available
2021-01-04T11:47:23Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/28900
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-28649
dc.description.abstract
Dynamic structural transitions within the seven-transmembrane bundle represent the mechanism by which G-protein-coupled receptors convert an extracellular chemical signal into an intracellular biological function. Here, the conformational dynamics of the neuropeptide Y receptor type 2 (Y2R) during activation was investigated. The apo, full agonist-, and arrestin-bound states of Y2R were prepared by cell-free expression, functional refolding, and reconstitution into lipid membranes. To study conformational transitions between these states, all six tryptophans of Y2R were(13)C-labeled. NMR-signal assignment was achieved by dynamic-nuclear-polarization enhancement and the individual functional states of the receptor were characterized by monitoring(13)C NMR chemical shifts. Activation of Y2R is mediated by molecular switches involving the toggle switch residue Trp281(6.48)of the highly conserved SWLP motif and Trp327(7.55)adjacent to the NPxxY motif. Furthermore, a conformationally preserved "cysteine lock"-Trp116(23.50)was identified.
en
dc.format.extent
8 Seiten
dc.rights.uri
https://creativecommons.org/licenses/by/4.0/
dc.subject
molecular switch
en
dc.subject
NMR spectroscopy
en
dc.subject
structural dynamics
en
dc.subject.ddc
500 Naturwissenschaften und Mathematik::540 Chemie::540 Chemie und zugeordnete Wissenschaften
dc.title
The Conformational Equilibrium of the Neuropeptide Y2 Receptor in Bilayer Membranes
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation.doi
10.1002/anie.202006075
dcterms.bibliographicCitation.journaltitle
Angewandte Chemie International Edition
dcterms.bibliographicCitation.number
52
dcterms.bibliographicCitation.pagestart
23854
dcterms.bibliographicCitation.pageend
23861
dcterms.bibliographicCitation.volume
59
dcterms.bibliographicCitation.url
https://doi.org/10.1002/anie.202006075
refubium.affiliation
Physik
refubium.resourceType.isindependentpub
no
dcterms.accessRights.openaire
open access
dcterms.isPartOf.issn
1433-7851
dcterms.isPartOf.eissn
1521-3773
refubium.resourceType.provider
WoS-Alert