3ILA
Crystal structure of rabbit ryanodine receptor 1 N-terminal domain (9-205)
Summary for 3ILA
| Entry DOI | 10.2210/pdb3ila/pdb |
| Descriptor | Ryanodine receptor 1 (1 entity in total) |
| Functional Keywords | beta trefoil, calcium channel, calcium transport, glycoprotein, ion transport, ionic channel, membrane, phosphoprotein, receptor, s-nitrosylation, transmembrane, transport, signaling protein |
| Biological source | Oryctolagus cuniculus (European rabbit,Japanese white rabbit,domestic rabbit,rabbits) |
| Cellular location | Membrane; Multi-pass membrane protein (Potential): P11716 |
| Total number of polymer chains | 9 |
| Total formula weight | 195944.89 |
| Authors | Lobo, P.A.,Van Petegem, F. (deposition date: 2009-08-06, release date: 2009-11-17, Last modification date: 2024-04-03) |
| Primary citation | 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 Cited by 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: 19913485DOI: 10.1016/j.str.2009.08.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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