Cryo-EM structure of human type-3 inositol triphosphate receptor reveals the presence of a self-binding peptide that acts as an antagonist

• Published in: The Journal of biological chemistry Vol. 295; no. 6; pp. 1743 - 1753
• Main Authors: Azumaya, Caleigh M., Linton, Emily A., Risener, Caitlin J., Nakagawa, Terunaga, Karakas, Erkan
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 07.02.2020; American Society for Biochemistry and Molecular Biology
• Subjects: Binding Sites; calcium channel; calcium intracellular release; Calcium Signaling; cell signaling; cryo-electron microscopy; Cryoelectron Microscopy; Humans; Inositol 1,4,5-Trisphosphate - metabolism; Inositol 1,4,5-Trisphosphate Receptors - antagonists & inhibitors; Inositol 1,4,5-Trisphosphate Receptors - chemistry; Inositol 1,4,5-Trisphosphate Receptors - metabolism; Inositol 1,4,5-Trisphosphate Receptors - ultrastructure; inositol trisphosphate receptor (InsP3R); ion channel; isothermal titration calorimetry (ITC); Models, Molecular; Peptides - metabolism; Protein Conformation; Protein Structure and Folding; self-binding peptide; structural biology; calcium channel; ion channel; cell signaling; calcium intracellular release; inositol trisphosphate receptor (InsP3R); structural biology; self-binding peptide; isothermal titration calorimetry (ITC); cryo-electron microscopy

Calcium-mediated signaling through inositol 1,4,5-triphosphate receptors (IP3Rs) is essential for the regulation of numerous physiological processes, including fertilization, muscle contraction, apoptosis, secretion, and synaptic plasticity. Deregulation of IP3Rs leads to pathological calcium signal...