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- W2038152032 abstract "Two recent X‐ray structures have tremendously increased the understanding of the sarco/endoplasmic reticulum Ca 2+ ‐ATPase (SERCA) and related proteins. Both structures show the fifth transmembrane span (M5) as a single continuous α‐helix. The inherent structural and dynamic features of this span (Lys758–Glu785) were studied in isolation in sodium dodecyl sulfate (SDS) micelles using liquid‐state nuclear magnetic resonance (NMR) spectroscopy. We find that a flexible region (Ile765–Asn768) is interrupting the α‐helix. The location of the flexible region near the Ca 2+ binding residues Asn768 and Glu771 suggests that together with a similar region in M6 it has a hinge function that may be important for cooperative Ca 2+ binding and occlusion." @default.
- W2038152032 created "2016-06-24" @default.
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- W2038152032 date "2003-05-06" @default.
- W2038152032 modified "2023-10-14" @default.
- W2038152032 title "NMR studies of the fifth transmembrane segment of sarcoplasmic reticulum Ca<sup>2+</sup>-ATPase reveals a hinge close to the Ca<sup>2+</sup>-ligating residues" @default.
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- W2038152032 doi "https://doi.org/10.1016/s0014-5793(03)00448-4" @default.
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