Journal
STRUCTURE
Volume 19, Issue 8, Pages 1192-1199Publisher
CELL PRESS
DOI: 10.1016/j.str.2011.05.003
Keywords
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Funding
- NIH [P41RR002250, R01GM072804, R01GM080139, RGM072804Z]
- MDA [88677]
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Inositol 1,4,5-trisphosphate receptors (IP(3)Rs) play a fundamental role in generating Ca2+ signals that trigger many cellular processes in virtually all eukaryotic cells. Thus far, the three-dimensional (3D) structure of these channels has remained extremely controversial. Here, we report a subnanometer resolution electron cryomicroscopy (cryo-EM) structure of a fully functional type 1 IP3R from cerebellum in the closed state. The transmembrane region reveals a twisted bundle of four a helices, one from each subunit, that form a funnel shaped structure around the 4-fold symmetry axis, strikingly similar to the ion-conduction pore of K+ channels. The lumenal face of IP(3)R1 has prominent densities that surround the pore entrance and similar to the highly structured turrets of Kir channels. 3D statistical analysis of the cryo-EM density map identifies high variance in the cytoplasmic region. This structural variation could be attributed to genuine structural flexibility of IP(3)R1.
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