Journal Article/Contribution to a conference proceedings

FZJ-2016-04537

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Internal sodium in GPCRs strongly responds to transmembrane voltage changes

Vickery, O. N. ; Machtens, J.-P.FZJ* ; Tamburrino, G. ; Seeliger, D. ; Zachariae, U.

2016
Cell Press Cambridge, Mass.

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Please use a persistent id in citations: doi:10.1016/j.bpj.2015.11.2300

Abstract: G protein-coupled receptors (GPCRs) are the largest superfamily of membrane proteins in the human genome, mediating the propagation of extracellular ligand binding information into intracellular signal transduction cascades. Crystal structures have revealed a water-filled hydrophilic internal pocket within their transmembrane domain, extending from the orthosteric ligand-binding site to regions near the G protein binding site. Recent high-resolution structures have identified a sodium ion near the base of this pocket, coordinated by highly conserved residues (1,2).

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Contributing Institute(s):

1. Zelluläre Biophysik (ICS-4)

Research Program(s):

1. 551 - Functional Macromolecules and Complexes (POF3-551) (POF3-551)

Appears in the scientific report 2016

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Database coverage:
; BIOSIS Previews ; Current Contents - Life Sciences ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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