9YLI
IP3/ATP-bound human type 2 IP3 receptor in the preactivated state
This is a non-PDB format compatible entry.
Summary for 9YLI
| Entry DOI | 10.2210/pdb9yli/pdb |
| EMDB information | 73054 7306 73088 |
| Descriptor | Inositol 1,4,5-trisphosphate-gated calcium channel ITPR2, D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | inositol 1, 4, 5-triphosphate, ip3, receptor, calcium channel, type-2, ip3r, ip3r-2, itpr2, transport protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 1263614.99 |
| Authors | |
| Primary citation | Liu, C.,Lan, Y.J.,Kushner, M.G.,Tang, Q.,Karakas, E. Conformational landscape and ligand-dependent clustering of the human type 2 IP 3 receptor. Nat Commun, 2026 Cited by PubMed Abstract: Inositol 1,4,5-trisphosphate (IP) receptors (IPRs) are tetrameric ER Ca channels that shape intracellular Ca signaling in response to IP, regulating diverse physiological processes. The structural basis for subtype-specific regulation among the three subtypes (IPR-1-3) remains incompletely understood due to the lack of IPR-2 structures. Here, we report cryo-electron microscopy (cryo-EM) structures of human IPR-2 in distinct conformations in the presence and absence of IP, Ca, and ATP. These structures define the conformational landscape of IPR-2, delineate ligand-binding interactions, and reveal shared architectural features alongside isoform-specific differences. We also resolve ligand-dependent IPR-2 assemblies, identifying a conformation-dependent inter-channel interface. Live-cell imaging demonstrates that IPR-2 undergoes clustering following ligand-induced Ca release, and disruption of this interface selectively abolishes clustering without impairing channel activity. Together, these findings provide a structural framework for human IPR-2 and establish a mechanism linking ligand-dependent conformational changes to inter-channel interactions and post-activation cellular clustering. PubMed: 42315508DOI: 10.1038/s41467-026-74494-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.33 Å) |
Structure validation
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