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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

Record type: Article

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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Citation

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), pp. 90-96. (doi:10.1016/j.bbamem.2011.09.017). (PMID:21963409).

More information

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 Philip T.F. Williamson: ORCID iD orcid.org/0000-0002-0231-8640

Catalogue record

Date deposited: 28 Oct 2011 10:50
Last modified: 18 Jul 2017 11:13

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