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TitleVisualization of the domain structure of an L-type Ca2+ channel using electron cryo-microscopy.
Journal, issue, pagesJ Mol Biol, Vol. 332, Issue 1, Page 171-182, Year 2003
Publish dateSep 5, 2003
AuthorsM Wolf / A Eberhart / H Glossmann / J Striessnig / N Grigorieff /
PubMed AbstractThe three-dimensional structure of the skeletal muscle voltage-gated L-type calcium channel (Ca(v)1.1; dihydropyridine receptor, DHPR) was determined using electron cryo-microscopy and single- ...The three-dimensional structure of the skeletal muscle voltage-gated L-type calcium channel (Ca(v)1.1; dihydropyridine receptor, DHPR) was determined using electron cryo-microscopy and single-particle averaging. The structure shows a single channel complex with an approximate total molecular mass of 550 kDa, corresponding to the five known subunits of the DHPR, and bound detergent and lipid. Features visible in our structure together with antibody labeling of the beta and alpha(2) subunits allowed us to assign locations for four of the five subunits within the structure. The most striking feature of the structure is the extra-cellular alpha(2) subunit that protrudes from the membrane domain in close proximity to the alpha(1) subunit. The cytosolic beta subunit is located close to the membrane and adjacent to subunits alpha(1), gamma and delta. Our structure correlates well with the functional and biochemical data available for this channel and suggests a three-dimensional model for the excitation-contraction coupling complex consisting of DHPR tetrads and the calcium release channel.
External linksJ Mol Biol / PubMed:12946355
MethodsEM (single particle)
Resolution21.0 Å
Structure data

EMDB-1069:
Visualization of the domain structure of an L-type Ca2+ channel using electron cryo-microscopy.
Method: EM (single particle) / Resolution: 21.0 Å

Source
  • Oryctolagus cuniculus (rabbit)

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