Structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with its ligand

Ivan Bosanac, Jean-René Alattia, Tapas K. Mal, Jenny Chan, Susanna Talarico, Frances K. Tong, Kit I. Tong, Fumio Yoshikawa, Teiichi Furuichi, Miwako Iwai, Takayuki Michikawa, Katsuhiko Mikoshiba and Mitsuhiko Ikura ()
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Ivan Bosanac: University of Toronto
Jean-René Alattia: University of Toronto
Tapas K. Mal: University of Toronto
Jenny Chan: University of Toronto
Susanna Talarico: University of Toronto
Frances K. Tong: University of Toronto
Kit I. Tong: University of Toronto
Fumio Yoshikawa: Brain Science Institute, RIKEN
Teiichi Furuichi: Brain Science Institute, RIKEN
Miwako Iwai: University of Tokyo
Takayuki Michikawa: University of Tokyo
Katsuhiko Mikoshiba: Brain Science Institute, RIKEN
Mitsuhiko Ikura: University of Toronto

Nature, 2002, vol. 420, issue 6916, 696-700

Abstract: Abstract In a variety of cells, the Ca2+ signalling process is mediated by the endoplasmic-reticulum-membrane-associated Ca2+ release channel, inositol 1,4,5-trisphosphate (InsP3) receptor (InsP3R)1. Being ubiquitous and present in organisms ranging from humans to Caenorhabditis elegans, InsP3R has a vital role in the control of cellular and physiological processes as diverse as cell division, cell proliferation, apoptosis, fertilization, development, behaviour, memory and learning2. Mouse type I InsP3R (InsP3R1), found in high abundance in cerebellar Purkinje cells, is a polypeptide with three major functionally distinct regions: the amino-terminal InsP3-binding region, the central modulatory region and the carboxy-terminal channel region2. Here we present a 2.2-Å crystal structure of the InsP3-binding core of mouse InsP3R1 in complex with InsP3. The asymmetric, boomerang-like structure consists of an N-terminal β-trefoil domain and a C-terminal α-helical domain containing an ‘armadillo repeat’-like fold. The cleft formed by the two domains exposes a cluster of arginine and lysine residues that coordinate the three phosphoryl groups of InsP3. Putative Ca2+-binding sites are identified in two separate locations within the InsP3-binding core.

Date: 2002
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DOI: 10.1038/nature01268

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