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2XKY

Single particle analysis of Kir2.1NC_4 in negative stain

Summary for 2XKY
Entry DOI10.2210/pdb2xky/pdb
Related1U4F 2GIX
EMDB information1764 1765 1766
DescriptorINWARD RECTIFIER POTASSIUM CHANNEL 2 (1 entity in total)
Functional Keywordsion channel, metal transport, membrane protein
Biological sourceMUS MUSCULUS (MOUSE)
Total number of polymer chains4
Total formula weight139921.09
Authors
Fomina, S.,Howard, T.D.,Sleator, O.K.,Golovanova, M.,O'Ryan, L.,Leyland, M.L.,Grossmann, J.G.,Collins, R.F.,Prince, S.M. (deposition date: 2010-07-15, release date: 2011-07-20, Last modification date: 2024-05-08)
Primary citationFomina, S.,Howard, T.D.,Sleator, O.K.,Golovanova, M.,O'Ryan, L.,Leyland, M.L.,Grossmann, J.G.,Collins, R.F.,Prince, S.M.
Self-Directed Assembly and Clustering of the Cytoplasmic Domains of Inwardly Rectifying Kir2.1 Potassium Channels on Association with Psd-95
Biochim.Biophys.Acta, 1808:2374-, 2011
Cited by
PubMed 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.
PubMed: 21756874
DOI: 10.1016/J.BBAMEM.2011.06.021
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (17.2 Å)
SOLUTION SCATTERING (17.2 Å)
Structure validation

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