3ILA

Crystal structure of rabbit ryanodine receptor 1 N-terminal domain (9-205)

3ILA の概要

• エントリーDOI: 10.2210/pdb3ila/pdb
• 分子名称: Ryanodine receptor 1 (1 entity in total)
• 機能のキーワード: beta trefoil, calcium channel, calcium transport, glycoprotein, ion transport, ionic channel, membrane, phosphoprotein, receptor, s-nitrosylation, transmembrane, transport, signaling protein
• 由来する生物種: Oryctolagus cuniculus (European rabbit,Japanese white rabbit,domestic rabbit,rabbits)
• 細胞内の位置: Membrane; Multi-pass membrane protein (Potential): P11716
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 195944.89

構造登録者

Lobo, P.A.,Van Petegem, F. (登録日: 2009-08-06, 公開日: 2009-11-17, 最終更新日: 2024-04-03)

主引用文献

Lobo, P.A.,Van Petegem, F.
Crystal structures of the N-terminal domains of cardiac and skeletal muscle ryanodine receptors: insights into disease mutations.
Structure, 17:1505-1514, 2009

PubMed Abstract: Ryanodine receptors (RyRs) are channels governing the release of Ca(2+) from the sarcoplasmic or endoplasmic reticulum. They are required for the contraction of both skeletal (RyR1) and cardiac (RyR2) muscles. Mutations in both RyR1 and RyR2 have been associated with severe genetic disorders, but high-resolution data describing the disease variants in detail have been lacking. Here we present the crystal structures of the N-terminal domains of both RyR2 (1-217) and RyR1 (9-205) at 2.55 A and 2.9 A, respectively. The domains map in a hot spot region for disease mutations. Both structures consist of a core beta trefoil domain flanked by an alpha helix. Crystal structures of two RyR2 disease mutants, A77V (2.2 A) and V186M (1.7 A), show that the mutations cause distinct local changes in the surface of the protein. A RyR2 deletion mutant causes significant changes in the thermal stability. The disease positions highlight two putative binding interfaces required for normal RyR function.

PubMed: 19913485
DOI: 10.1016/j.str.2009.08.016

実験手法

X-RAY DIFFRACTION (2.9 Å)