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9C1F

Mink RyR3 in open conformation bound to Ca2+/ATP/caffeine

これはPDB形式変換不可エントリーです。
9C1F の概要
エントリーDOI10.2210/pdb9c1f/pdb
EMDBエントリー45117
分子名称Peptidyl-prolyl cis-trans isomerase FKBP1B, Ryanodine receptor 3, ZINC ION, ... (7 entities in total)
機能のキーワードryr3, ryanodine receptor, calcium channel, ion channel, membrane protein
由来する生物種Homo sapiens (human)
詳細
タンパク質・核酸の鎖数8
化学式量合計2258025.72
構造登録者
Chen, Y.S.,Van Petegem, F. (登録日: 2024-05-29, 公開日: 2024-10-16, 最終更新日: 2024-11-20)
主引用文献Chen, Y.S.,Garcia-Castaneda, M.,Charalambous, M.,Rossi, D.,Sorrentino, V.,Van Petegem, F.
Cryo-EM investigation of ryanodine receptor type 3.
Nat Commun, 15:8630-8630, 2024
Cited by
PubMed Abstract: Ryanodine Receptor isoform 3 (RyR3) is a large ion channel found in the endoplasmic reticulum membrane of many different cell types. Within the hippocampal region of the brain, it is found in dendritic spines and regulates synaptic plasticity. It controls myogenic tone in arteries and is upregulated in skeletal muscle in early development. RyR3 has a unique functional profile with a very high sensitivity to activating ligands, enabling high gain in Ca-induced Ca release. Here we solve high-resolution cryo-EM structures of RyR3 in non-activating and activating conditions, revealing structural transitions that occur during channel opening. Addition of activating ligands yields only open channels, indicating an intrinsically high open probability under these conditions. RyR3 has reduced binding affinity to the auxiliary protein FKBP12.6 due to several sequence variations in the binding interface. We map disease-associated sequence variants and binding sites for known pharmacological agents. The N-terminal region contains ligand binding sites for a putative chloride anion and ATP, both of which are targeted by sequence variants linked to epileptic encephalopathy.
PubMed: 39366997
DOI: 10.1038/s41467-024-52998-9
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.22 Å)
構造検証レポート
Validation report summary of 9c1f
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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