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- W3005259093 abstract "Calcium (Ca2+) dysregulation is a hallmark of heart failure and is characterized by impaired Ca2+ sequestration into the sarcoplasmic reticulum (SR) by the SR-Ca2+-ATPase (SERCA). Regulins, single-pass membrane proteins, bind and inhibit SERCA by allosterically modulating the affinity of its Ca2+ binding sites. DWarf Open Reading Frame (DWORF) is a 35 amino acid regulin that enhances SERCA2a activity in cardiomyocytes. As a first step to understanding DWORF regulation of SERCA, we used Oriented-Sample Solid-State NMR spectroscopy (OS-ssNMR) and computational methods to determine the structure and topology of DWORF in liquid crystalline lipid bilayers. We found that DWORF adopts a helical structure, with a pronounced kink at the N-terminus. Restrained molecular dynamics calculations using backbone dipolar couplings and chemical shift anisotropy show the dynamic topology of DWORF, with the N-terminal helix spanning tilt angles ranging from 50-60 degrees and C-terminal helix ranging from 30-40 degrees. The two helical domains are anchored to both membrane leaflets by polar residues. This topology differs from that of phospholamban, a main regulator of SERCA, and might explain the opposite effects on the ATPase's apparent affinity for Ca2+ ions of these two regulins." @default.
- W3005259093 created "2020-02-14" @default.
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- W3005259093 date "2020-02-01" @default.
- W3005259093 modified "2023-09-27" @default.
- W3005259093 title "Structure and Topology of the SERCA Regulator DWORF in Lipid Bilayers by Oriented Sample Solid-State NMR" @default.
- W3005259093 doi "https://doi.org/10.1016/j.bpj.2019.11.1249" @default.
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