2XKX

Single particle analysis of PSD-95 in negative stain

Summary for 2XKX

• Entry DOI: 10.2210/pdb2xkx/pdb
• Related: 1BE9 1BFE 1IU0 1IU2 1JXM 1JXO 1KJW 1QLC 1RGR 1TP3 1TP5 1TQ3 2XKY
• EMDB information: 1761
• Descriptor: DISKS LARGE HOMOLOG 4 (1 entity in total)
• Functional Keywords: structural protein, scaffold protein, membrane associated guanylate kinase
• Biological source: RATTUS NORVEGICUS (NORWAY RAT)
• Total number of polymer chains: 2
• Total formula weight: 160406.09

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 citation

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.
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

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

Experimental method

ELECTRON MICROSCOPY (22.9 Å)
SOLUTION SCATTERING (22.9 Å)