Inositol trisphosphate receptor
|inositol 1,4,5-trisphosphate receptor, type 1|
Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor
|Locus||Chr. 3 p26.1|
|inositol 1,4,5-trisphosphate receptor, type 2|
|HUGO||structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor 6181 Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor 6181|
|Locus||Chr. 12 p11.23|
|inositol 1,4,5-trisphosphate receptor, type 3|
|Locus||Chr. 6 p21.31|
Inositol trisphosphate receptor (InsP3R) is a membrane
- Inositol Trisphosphate Receptor at the US National Library of Medicine Medical Subject Headings (MeSH)
- Bosanac I, Yamazaki H, Matsu-Ura T, Michikawa T, Mikoshiba K, Ikura M (January 2005). "Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor". Mol. Cell 17 (2): 193–203.
- Bosanac I, Alattia JR, Mal TK, et al. (December 2002). "Structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with its ligand". Nature 420 (6916): 696–700.
- Yoshida Y, Imai S (June 1997). "Structure and function of inositol 1,4,5-trisphosphate receptor". Jpn. J. Pharmacol. 74 (2): 125–37.
- Supattapone S, et al. J Biol Chem. 1988 Jan 25;263(3):1530-4.
- inositol phosphate
- MRVI1 associated through complex formation.
The asymmetric structure consists of an N-terminal beta-trefoil domain and a C-terminal alpha helical domain with a folding pattern similar to an armadillo repeat fold. The split formed by the two terminals contains multiple arginine and lysine residues that coordinate the three phosphoryl groups of InsP3. The InsP3R complex is formed of four 313 kDa subunits. In amphibians, fish and mammals there are 3 paralogs and these can form homo- or hetero-oligomers. InsP3R-1 is the most widely expressed of these three and is found in all tissue types and all developmental stages of life. It is additionally the means for further InsP3 receptor diversity in that it has as many as four splice sites with as many as 9 different optional exons or exon variants. Combinations of these can be introduced into a given transcript in order to modulate its pharmacological activity.
- Distribution 1
- Structure 2
- See also 3
- References 4
- External links 5
 The InsP3 receptor was first purified from rat cerebellum by neuroscientists Surachai Supattapone and Solomon Snyder at Johns Hopkins University School of Medicine.  waves and oscillations.2+ signals characterized by complex patterns relative to both space and time. For example, Ca2+ from intracellular store sites. There is strong evidence suggesting that the InsP3R plays an important role in the conversion of external stimuli to intracellular Ca2+ Inositol triphosphate receptor represents a dominant second messenger leading to the release of Ca