ArticleNature structural & molecular biology2011
Apo and InsP₃-bound crystal structures of the ligand-binding domain of an InsP₃ receptor.
Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- Cryo-EM insights into isoform-specific properties of the IPNature communications · 2026Article
- Conformational landscape and ligand-dependent clustering of the human type 2 IPNature communications · 2026Article
- Structural titration reveals CaNature communications · 2023Article
- Understanding IPCell calcium · 2023Review
- Conformational motions and ligand-binding underlying gating and regulation in IPNature communications · 2022Article
- Functional determination of calcium-binding sites required for the activation of inositol 1,4,5-trisphosphate receptors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural basis for activation and gating of IPNature communications · 2022Article
- Structural Insight Into Ryanodine Receptor Channelopathies.Frontiers in pharmacology · 2022Review
- 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
- The discovery and development of IP3 receptor modulators: an update.Expert opinion on drug discovery · 2021Article
- Article
- Inositol 1,4,5-Trisphosphate Receptors in Human Disease: A Comprehensive Update.Journal of clinical medicine · 2020Review
- Bcl-2-Protein Family as Modulators of IPCold Spring Harbor perspectives in biology · 2020Review
- Bcl-2 and IPCellular and molecular life sciences : CMLS · 2019Article
- Structure and Function of IPCold Spring Harbor perspectives in biology · 2019Review
- Exploration of inositol 1,4,5-trisphosphate (IPScientific reports · 2019Article
- Allosteric response to ligand binding: Molecular dynamics study of the N-terminal domains in IPBiophysics and physicobiology · 2019Article
- Cryo-EM reveals ligand induced allostery underlying InsPCell research · 2018Article
- Aberrant IPProceedings of the National Academy of Sciences of the United States of America · 2018Article
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Authors and funding
3 authors.
Funding
Abstract
We report the crystal structures of the ligand-binding domain (LBD) of a rat inositol 1,4,5-trisphosphate receptor (InsP(3)R) in its apo and InsP(3)-bound conformations. Comparison of these two conformations reveals that LBD's first β-trefoil fold (β-TF1) and armadillo repeat fold (ARF) move together as a unit relative to its second β-trefoil fold (β-TF2). Whereas apo LBD may spontaneously transition between gating conformations, InsP(3) binding shifts this equilibrium toward the active state.
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