Three-dimensional structure of the type 1 inositol 1,4,5-trisphosphate receptor at 24 Å resolution

Qiu Xing Jiang, Edwin C. Thrower, David W. Chester, Barbara E. Ehrlich, Fred J. Sigworth

Research output: Contribution to journalArticlepeer-review

101 Scopus citations


We report here the first three-dimensional structure of the type 1 inositol 1,4,5-trisphosphate receptor (IP3R). From cryo-electron microscopic images of purified receptors embedded in vitreous ice, a three-dimensional structure was determined by use of standard single particle reconstruction techniques. The structure is strikingly different from that of the ryanodine receptor at similar resolution despite molecular similarities between these two calcium release channels. The 24 Å resolution structure of the IP3R takes the shape of an uneven dumbbell, and is ∼170 Å tall. Its larger endq is bulky, with four arms protruding laterally by ∼50 Å and, in comparison with the receptor topology, probably corresponds to the cytoplasmic domain of the receptor. The lateral dimension at the height of the protruding arms is ∼155 Å. The smaller end, whose lateral dimension is ∼100 Å, has structural features indicative of the membrane-spanning domain. A central opening in this domain, which is occluded on the cytoplasmic half, outlines a pathway for calcium flow in the open state of the channel.

Original languageEnglish (US)
Pages (from-to)3575-3581
Number of pages7
JournalEMBO Journal
Issue number14
StatePublished - Jul 15 2002


  • Channel
  • Cryo-electron microscopy
  • IP receptor
  • Single particle reconstruction

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)


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