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- W180994966 abstract "Publisher Summary Inositol 1,4,5-trisphosphate receptors (IP 3 Rs) are a family of ligand-gated channels that release calcium primarily from endoplasmic reticulum stores. To elucidate the structure and regulation of IP 3 R channels at the molecular level is of paramount importance to understand the disease progression and the development of targeted therapeutics. This chapter discusses and examines the molecular architecture of the transmembrane domains and the channel pore. The IP 3 R channel is a tetramer that forms a single ion conduction pore. It is generally accepted that all cells express at least one IP 3 R isoform and most tissues express a combination of isoforms, which can form homo- and heterotetramers. There are two atomic resolution structures of parts of the IP 3 R protein: the ligand binding domain, and the suppressor region. The ligand binding domain is formed by a pocket sandwiched between a beta-trefoil domain and an armadillo-like repeat. The suppressor domain also has a beta-trefoil like fold, and likely interacts with and stabilizes the IP 3 binding core. Significant advances are made in understanding structural and functional relationships in the channel domain using biochemistry and electrophysiology." @default.
- W180994966 created "2016-06-24" @default.
- W180994966 creator A5077835261 @default.
- W180994966 date "2010-01-01" @default.
- W180994966 modified "2023-09-23" @default.
- W180994966 title "Molecular Architecture of the Inositol 1,4,5-Trisphosphate Receptor Pore" @default.
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- W180994966 doi "https://doi.org/10.1016/s1063-5823(10)66009-7" @default.
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