1n4k
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Crystal structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with IP3
OverviewOverview
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). 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, (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 region. Here we present a 2.2-A crystal structure, of the InsP3-binding core of mouse InsP3R1 in complex with InsP3. The, asymmetric, boomerang-like structure consists of an N-terminal, beta-trefoil domain and a C-terminal alpha-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.
About this StructureAbout this Structure
1N4K is a Single protein structure of sequence from Mus musculus with I3P as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with its ligand., Bosanac I, Alattia JR, Mal TK, Chan J, Talarico S, Tong FK, Tong KI, Yoshikawa F, Furuichi T, Iwai M, Michikawa T, Mikoshiba K, Ikura M, Nature. 2002 Dec 12;420(6916):696-700. Epub 2002 Nov 17. PMID:12442173
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