Publications by authors named "Alexander B Seryshev"
Inositol-1,4,5-trisphosphate receptors (IPRs) are activated by IP and Ca and their gating is regulated by various intracellular messengers that finely tune the channel activity. Here, using single particle cryo-EM analysis we determined 3D structures of the nanodisc-reconstituted IPR1 channel in two ligand-bound states. These structures provide unprecedented details governing binding of IP, Ca and ATP, revealing conformational changes that couple ligand-binding to channel opening.
View Article and Find Full Text PDFType 1 inositol 1,4,5-trisphosphate receptor (IPR1) is the predominant Ca-release channel in neurons. IPR1 mediates Ca release from the endoplasmic reticulum into the cytosol and thereby is involved in many physiological processes. Here, we present the cryo-EM structures of full-length rat IPR1 reconstituted in lipid nanodisc and detergent solubilized in the presence of phosphatidylcholine determined in ligand-free, closed states by single-particle electron cryo-microscopy.
View Article and Find Full Text PDFArticle Synopsis
- Inositol-1,4,5-trisphosphate receptors (InsPRs) are cation channels that regulate calcium release from cell stores when activated by various signals.
- The study presents the electron cryo-microscopy structures of InsPR1 from rat cerebellum, providing insights into how calcium and a specific agonist (adenophostin A) influence the receptor's gate opening and closing.
- The findings reveal how ligand-binding leads to conformational changes in the receptor, which aid in understanding the mechanisms of InsPR activation and the regulation of calcium signaling in cells.