7RW4

Crystal structure of junctophilin-1

Summary for 7RW4

• Entry DOI: 10.2210/pdb7rw4/pdb
• Descriptor: Junctophilin-1, ACETATE ION, GLYCEROL, ... (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: 38415.32

Authors

Yang, Z.,Panwar, P.,Van Petegem, F. (deposition date: 2021-08-19, release date: 2022-02-23, Last modification date: 2024-05-22)

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

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: 35238659
DOI: 10.1073/pnas.2120416119

Experimental method

X-RAY DIFFRACTION (1.31 Å)