7RXE
Crystal structure of junctophilin-2
Summary for 7RXE
| Entry DOI | 10.2210/pdb7rxe/pdb |
| Related | 7RW4 |
| Descriptor | Junctophilin-2 N-terminal fragment, ISOPROPYL ALCOHOL, CITRATE ANION, ... (4 entities in total) |
| Functional Keywords | muscle, membrane, ion channel, structural protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 36492.09 |
| Authors | Yang, Z.,Panwar, P.,Van Petegem, F. (deposition date: 2021-08-22, release date: 2022-02-23, Last modification date: 2023-10-18) |
| Primary citation | Yang, Z.F.,Panwar, P.,McFarlane, C.R.,Tuinte, W.E.,Campiglio, M.,Van Petegem, F. Structures of the junctophilin/voltage-gated calcium channel interface reveal hot spot for cardiomyopathy mutations. Proc.Natl.Acad.Sci.USA, 119:e2120416119-e2120416119, 2022 Cited by PubMed Abstract: SignificanceIon channels have evolved the ability to communicate with one another, either through protein-protein interactions, or indirectly via intermediate diffusible messenger molecules. In special cases, the channels are part of different membranes. In muscle tissue, the T-tubule membrane is in proximity to the sarcoplasmic reticulum, allowing communication between L-type calcium channels and ryanodine receptors. This process is critical for excitation-contraction coupling and requires auxiliary proteins like junctophilin (JPH). JPHs are targets for disease-associated mutations, most notably hypertrophic cardiomyopathy mutations in the JPH2 isoform. Here we provide high-resolution snapshots of JPH, both alone and in complex with a calcium channel peptide, and show how this interaction is targeted by cardiomyopathy mutations. PubMed: 35238659DOI: 10.1073/pnas.2120416119 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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