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, Mitsuhiko Ikura

Research output: Contribution to journalArticlepeer-review

289 Scopus citations


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 learning. Mouse type I InsP3R (InsP3RI), 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 region. Here we present a 2.2-Å crystal structure of the InsP3-binding core of mouse InSP3RI 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.

Original languageEnglish (US)
Pages (from-to)696-700
Number of pages5
Issue number6916
StatePublished - Dec 12 2002

All Science Journal Classification (ASJC) codes

  • General


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