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Probing the interaction of lipids with the non-annular binding sites of the potassium channel KcsA by magic-angle spinning NMR

Probing the interaction of lipids with the non-annular binding sites of the potassium channel KcsA by magic-angle spinning NMR
Probing the interaction of lipids with the non-annular binding sites of the potassium channel KcsA by magic-angle spinning NMR
The activity of the potassium channel, KcsA is tightly regulated through the interactions of anionic lipids with high-affinity non-annular lipid binding sites located at the interface between the channel's subunits. Here we present solid-state phosphorous NMR studies that resolve the negatively charged lipid phosphatidylglycerol within the non-annular lipid-binding site. Perturbations in chemical shift observed upon the binding of phosphatidylglycerol are indicative of the interaction of positively charged sidechains within the non-annular binding site and the negatively charged lipid headgroup. Site directed mutagenesis studies have attributed these charge interactions to R64 and R89. Functionally the removal of the positive charges from R64 and R89 appears to act synergistically to reduce the probability of channel opening
0304-4165
90-96
Marius, Phedra
f5bf8a27-2332-4d04-a45b-4b2677fcc865
de Planque, Maurits R.R.
a1d33d13-f516-44fb-8d2c-c51d18bc21ba
Williamson, Philip T.F.
0b7715c6-b60e-4e95-a1b1-6afc8b9f372a
Marius, Phedra
f5bf8a27-2332-4d04-a45b-4b2677fcc865
de Planque, Maurits R.R.
a1d33d13-f516-44fb-8d2c-c51d18bc21ba
Williamson, Philip T.F.
0b7715c6-b60e-4e95-a1b1-6afc8b9f372a

Marius, Phedra, de Planque, Maurits R.R. and Williamson, Philip T.F. (2012) Probing the interaction of lipids with the non-annular binding sites of the potassium channel KcsA by magic-angle spinning NMR. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1818 (1), 90-96. (doi:10.1016/j.bbamem.2011.09.017). (PMID:21963409)

Record type: Article

Abstract

The activity of the potassium channel, KcsA is tightly regulated through the interactions of anionic lipids with high-affinity non-annular lipid binding sites located at the interface between the channel's subunits. Here we present solid-state phosphorous NMR studies that resolve the negatively charged lipid phosphatidylglycerol within the non-annular lipid-binding site. Perturbations in chemical shift observed upon the binding of phosphatidylglycerol are indicative of the interaction of positively charged sidechains within the non-annular binding site and the negatively charged lipid headgroup. Site directed mutagenesis studies have attributed these charge interactions to R64 and R89. Functionally the removal of the positive charges from R64 and R89 appears to act synergistically to reduce the probability of channel opening

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e-pub ahead of print date: September 2011
Published date: January 2012
Organisations: Molecular and Cellular, Magnetic Resonance

Identifiers

Local EPrints ID: 201215
URI: http://eprints.soton.ac.uk/id/eprint/201215
ISSN: 0304-4165
PURE UUID: 59240b88-26c6-4d7f-b4a5-d1f48e454627
ORCID for Maurits R.R. de Planque: ORCID iD orcid.org/0000-0002-8787-0513
ORCID for Philip T.F. Williamson: ORCID iD orcid.org/0000-0002-0231-8640

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Date deposited: 28 Oct 2011 10:50
Last modified: 15 Mar 2024 03:27

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Contributors

Author: Phedra Marius
Author: Maurits R.R. de Planque ORCID iD

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