Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1808, Issue 10, Pages 2374-2389Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2011.06.021
Keywords
Potassium channel; MAGUK; Cluster; Electron microscopy; Small angle X-ray scattering
Categories
Funding
- Biotechnology and Biological Sciences Research Council [BBS/B/05567, A1/B/08277]
- Royal Society [23055]
- Engineering and Physical Sciences Research Council
- Biotechnology and Biological Sciences Research Council [BBS/B/05567] Funding Source: researchfish
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The interaction of the extra-membranous domain of tetrameric inwardly rectifying Kir2.1 ion channels (Kir2.1NC(4)) with the membrane associated guanylate kinase protein PSD-95 has been studied using Transmission Electron Microscopy in negative stain. Three types of complexes were observed in electron micrographs corresponding to a 1:1 complex, a large self-enclosed tetrad complex and extended chains of linked channel domains. Using models derived from small angle X-ray scattering experiments in which high resolution structures from X-ray crystallographic and Nuclear Magnetic Resonance studies are positioned, the envelopes from single particle analysis can be resolved as a Kir2.1NC(4):PSD-95 complex and a tetrad of this unit (Kir2.1NC(4):PSD-95)(4). The tetrad complex shows the close association of the Kir2.1 cytoplasmic domains and the influence of PSD-95 mediated self-assembly on the clustering of these channels. (C) 2011 Elsevier B.V. All rights reserved.
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