4ETT

Crystal structure of rabbit ryanodine receptor 1 mutant E2764K

4ETT の概要

• エントリーDOI: 10.2210/pdb4ett/pdb
• 関連するPDBエントリー: 4ERT 4ERV 4ESU 4ETU 4ETV
• 分子名称: Ryanodine receptor 1, GLYCEROL (3 entities in total)
• 機能のキーワード: ryanodine receptor calcium release channel, phosphorylation, muscle, skeletal, metal transport
• 由来する生物種: Oryctolagus cuniculus (rabbit)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25030.19

構造登録者

Yuchi, Z.,Lau, K.,Van Petegem, F. (登録日: 2012-04-24, 公開日: 2012-06-13, 最終更新日: 2023-09-13)

主引用文献

Yuchi, Z.,Lau, K.,Van Petegem, F.
Disease mutations in the ryanodine receptor central region: crystal structures of a phosphorylation hot spot domain.
Structure, 20:1201-1211, 2012

PubMed Abstract: Ryanodine Receptors (RyRs) are huge Ca²⁺ release channels in the endoplasmic reticulum membrane and form targets for phosphorylation and disease mutations. We present crystal structures of a domain in three RyR isoforms, containing the Ser2843 (RyR1) and Ser2808/Ser2814 (RyR2) phosphorylation sites. The RyR1 domain is the target for 11 disease mutations. Several of these are clustered near the phosphorylation sites, suggesting that phosphorylation and disease mutations may affect the same interface. The L2867G mutation causes a drastic thermal destabilization and aggregation at room temperature. Crystal structures for other disease mutants show that they affect surface properties and intradomain salt bridges. In vitro phosphorylation experiments show that up to five residues in one long loop of RyR2 can be phosphorylated by PKA or CaMKII. Docking into cryo-electron microscopy maps suggests a putative location in the clamp region, implying that mutations and phosphorylation may affect the allosteric motions within this area.

PubMed: 22705209
DOI: 10.1016/j.str.2012.04.015

実験手法

X-RAY DIFFRACTION (2.195 Å)