Structural highlights
Function
FKB1B_HUMAN Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Publication Abstract from PubMed
The type 1 ryanodine receptor (RyR)/calcium release channel on the sarcoplasmic reticulum (SR) is required for skeletal muscle excitation-contraction coupling and is the largest known ion channel, composed of four 565-kDa protomers. Cryogenic electron microscopy (cryo-EM) studies of the RyR have primarily used detergent to solubilize the channel; in the present study, we have used cryo-EM to solve high-resolution structures of the channel in liposomes using a gel-filtration approach with on-column detergent removal to form liposomes and incorporate the channel simultaneously. This allowed us to resolve the structure of the channel in the primed and open states at 3.4 and 4.0 A, respectively, with a single dataset. This method offers validation for detergent-based structures of the RyR and offers a starting point for utilizing a chemical gradient mimicking the SR, where Ca(2+) concentrations are millimolar in the lumen and nanomolar in the cytosol.
High-resolution structure of the membrane-embedded skeletal muscle ryanodine receptor.,Melville Z, Kim K, Clarke OB, Marks AR Structure. 2022 Jan 6;30(1):172-180.e3. doi: 10.1016/j.str.2021.08.001. Epub 2021 , Aug 31. PMID:34469755[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Melville Z, Kim K, Clarke OB, Marks AR. High-resolution structure of the membrane-embedded skeletal muscle ryanodine receptor. Structure. 2022 Jan 6;30(1):172-180.e3. PMID:34469755 doi:10.1016/j.str.2021.08.001
