EMD-1764
Single particle analysis of Kir2.1NC_4 in negative stain
EMD-1764
Single-particle17.2 Å
Deposition: 15/07/2010Map released: 14/07/2011
Last modified: 26/11/2014
Sample Organism:
Mus musculus
Sample: mouse Kir2.1, cytoplamic domain, homotetramer of fused N,C termini
Fitted models: 2xky (Avg. Q-score: -0.012)
Deposition Authors: Fomina S, Howard TD, Sleator OK, Golovanova M, O'Ryan L, Leyland M, Grossmann JG, Collins RF, Prince SM
Sample: mouse Kir2.1, cytoplamic domain, homotetramer of fused N,C termini
Fitted models: 2xky (Avg. Q-score: -0.012)
Deposition Authors: Fomina S, Howard TD, Sleator OK, Golovanova M, O'Ryan L, Leyland M, Grossmann JG, Collins RF, Prince SM
Self-directed assembly and clustering of the cytoplasmic domains of inwardly rectifying Kir2.1 potassium channels on association with PSD-95.
Fomina S,
Howard TD,
Sleator OK,
Golovanova M,
O'Ryan L,
Leyland ML,
Grossmann JG,
Collins RF,
Prince SM
(2011) Biochim Biophys Acta , 1808 , 2374 - 2389
(2011) Biochim Biophys Acta , 1808 , 2374 - 2389
Abstract:
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.
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.