Structural insights into the regulatory mechanism of IP3 receptor.
Inositol 1,4,5-trisphosphate receptors (IP(3)R) are intracellular Ca(2+) release channels whose opening requires binding of two intracellular messengers IP(3) and Ca(2+). The regulation of IP(3)R function has also been shown to involve a variety of cellular proteins. Recent biochemical and structural analyses have deepened our understanding of how the IP(3)-operated Ca(2+) channel functions. Specifically, the atomic resolution structure of the IP(3)-binding region has provided a sound structural basis for the receptor interaction with the natural ligand. Electron microscopic studies have also shed light on the overall shape of the tetrameric receptor. This review aims to provide comprehensive overview of the current information available on the structure and function relationship of IP(3)R.
Bosanac
Ivan
I
Division of Molecular and Structural Biology, Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, 610 University Avenue, Toronto, Ontario, Canada M5G 2M9.
Michikawa
Takayuki
T
Mikoshiba
Katsuhiko
K
Ikura
Mitsuhiko
M
D000595:Amino Acid Sequence; D000818:Animals; D015220:Calcium Channels / Q000737:chemistry* / Q000502:physiology* / Q000648:ultrastructure; D018360:Crystallography, X-Ray; D006801:Humans; D053496:Inositol 1,4,5-Trisphosphate Receptors; D008854:Microscopy, Electron; D008958:Models, Molecular; D008969:Molecular Sequence Data; D018160:Receptors, Cytoplasmic and Nuclear / Q000737:chemistry* / Q000502:physiology* / Q000648:ultrastructure; D017386:Sequence Homology, Amino Acid
D015220:Calcium Channels; C506926:ITPR1 protein, human; D053496:Inositol 1,4,5-Trisphosphate Receptors; D018160:Receptors, Cytoplasmic and Nuclear