ArticleThe Journal of biological chemistry2010
Structural studies of inositol 1,4,5-trisphosphate receptor: coupling ligand binding to channel gating.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Dominant negative variants in ITPR3 impair T cell Ca2+ dynamics causing combined immunodeficiency.The Journal of experimental medicine · 2025Article
- Combined Pharmacophore and Grid-Independent Molecular Descriptors (GRIND) Analysis to Probe 3D Features of Inositol 1,4,5-Trisphosphate Receptor (IPInternational journal of molecular sciences · 2021Article
- A Comparative Perspective on Functionally-Related, Intracellular Calcium Channels: The Insect Ryanodine and Inositol 1,4,5-Trisphosphate Receptors.Biomolecules · 2021Review
- Cryo-EM structure of human type-3 inositol triphosphate receptor reveals the presence of a self-binding peptide that acts as an antagonist.The Journal of biological chemistry · 2020Article
- Exploration of inositol 1,4,5-trisphosphate (IPScientific reports · 2019Article
- Redox regulation of type-I inositol trisphosphate receptors in intact mammalian cells.The Journal of biological chemistry · 2018Article
- Structural basis for the regulation of inositol trisphosphate receptors by CaNature structural & molecular biology · 2018Article
- Review
- Defining the stoichiometry of inositol 1,4,5-trisphosphate binding required to initiate Ca2+ release.Science signaling · 2016Article
- The type 2 inositol 1,4,5-trisphosphate receptor, emerging functions for an intriguing Ca²⁺-release channel.Biochimica et biophysica acta · 2015Review
- Regulatory Mechanisms of Endoplasmic Reticulum Resident IP3 Receptors.Journal of molecular neuroscience : MN · 2015Review
- Aberrant calcium signaling by transglutaminase-mediated posttranslational modification of inositol 1,4,5-trisphosphate receptors.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Intracellular calcium channels: inositol-1,4,5-trisphosphate receptors.European journal of pharmacology · 2014Review
- Toward a high-resolution structure of IP₃R channel.Cell calcium · 2014Review
- Basis for a neuronal version of Grover's quantum algorithm.Frontiers in molecular neuroscience · 2014Article
- Fragmented inositol 1,4,5-trisphosphate receptors retain tetrameric architecture and form functional Ca2+ release channels.The Journal of biological chemistry · 2013Article
- The selective BH4-domain biology of Bcl-2-family members: IP3Rs and beyond.Cellular and molecular life sciences : CMLS · 2013Review
- Stimulation of inositol 1,4,5-trisphosphate (IP3) receptor subtypes by analogues of IP3.PloS one · 2013Article
- Identification of functionally critical residues in the channel domain of inositol trisphosphate receptors.The Journal of biological chemistry · 2012Article
- Structural and functional conservation of key domains in InsP3 and ryanodine receptors.Nature · 2012Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The three isoforms of the inositol 1,4,5-trisphosphate receptor (IP(3)R) exhibit distinct IP(3) sensitivities and cooperativities in calcium (Ca(2+)) channel function. The determinants underlying this isoform-specific channel gating mechanism have been localized to the N-terminal suppressor region of IP(3)R. We determined the 1.9 Å crystal structure of the suppressor domain from type 3 IP(3)R (IP(3)R3(SUP), amino acids 1-224) and revealed structural features contributing to isoform-specific functionality of IP(3)R by comparing it with our previously determined structure of the type 1 suppressor domain (IP(3)R1(SUP)). The molecular surface known to associate with the ligand binding domain (amino acids 224-604) showed marked differences between IP(3)R3(SUP) and IP(3)R1(SUP). Our NMR and biochemical studies showed that three spatially clustered residues (Glu-20, Tyr-167, and Ser-217 in IP(3)R1 and Glu-19, Trp-168, and Ser-218 in IP(3)R3) within the N-terminal suppressor domains of IP(3)R1(SUP) and IP(3)R3(SUP) interact directly with their respective C-terminal fragments. Together with the accompanying paper (Yamazaki, H., Chan, J., Ikura, M., Michikawa, T., and Mikoshiba, K. (2010) J. Biol. Chem. 285, 36081-36091), we demonstrate that the single aromatic residue in this region (Tyr-167 in IP(3)R1 and Trp-168 in IP(3)R3) plays a critical role in the coupling between ligand binding and channel gating.
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