This title appears in the Scientific Report :
2016
Please use the identifier:
http://dx.doi.org/10.1016/j.bpj.2015.11.2300 in citations.
Internal sodium in GPCRs strongly responds to transmembrane voltage changes
Internal sodium in GPCRs strongly responds to transmembrane voltage changes
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...
Saved in:
Personal Name(s): | Vickery, O. N. |
---|---|
Machtens, Jan-Philipp / Tamburrino, G. / Seeliger, D. / Zachariae, U. | |
Contributing Institute: |
Zelluläre Biophysik; ICS-4 |
Published in: | Biophysical journal, 110 (2016) 3, S. 425a-426a |
Imprint: |
Cambridge, Mass.
Cell Press
2016
|
Physical Description: |
425a-426a |
DOI: |
10.1016/j.bpj.2015.11.2300 |
Conference: | 60th Annual Meeting of the Biophysical-Society, Los Angeles, CA (USA), 2016-02-27 - 2016-03-02 |
Document Type: |
Contribution to a conference proceedings Journal Article |
Research Program: |
Functional Macromolecules and Complexes |
Publikationsportal JuSER |
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). |