کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1944800 | 1053240 | 2010 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Solid-state 2H and 15N NMR studies of side-chain and backbone dynamics of phospholamban in lipid bilayers: Investigation of the N27A mutation Solid-state 2H and 15N NMR studies of side-chain and backbone dynamics of phospholamban in lipid bilayers: Investigation of the N27A mutation](/preview/png/1944800.png)
Phospholamban (PLB) is an integral membrane protein regulating Ca2+ transport through inhibitory interaction with sarco(endo)plasmic reticulum calcium ATPase (SERCA). The Asn27 to Ala (N27A) mutation of PLB has been shown to function as a superinhibitor of the affinity of SERCA for Ca2+ and of cardiac contractility in vivo. The effects of this N27A mutation on the side-chain and backbone dynamics of PLB were investigated with 2H and 15N solid-state NMR spectroscopy in phospholipid multilamellar vesicles (MLVs). 2H and 15N NMR spectra indicate that the N27A mutation does not significantly change the side-chain or backbone dynamics of the transmembrane and cytoplasmic domains when compared to wild-type PLB. However, dynamic changes are observed for the hinge region, in which greater mobility is observed for the CD3-labeled Ala24 N27A-PLB. The increased dynamics in the hinge region of PLB upon N27A mutation may allow the cytoplasmic helix to more easily interact with the Ca2+-ATPase; thus, showing increased inhibition of Ca2+-ATPase.
Journal: Biochimica et Biophysica Acta (BBA) - Biomembranes - Volume 1798, Issue 2, February 2010, Pages 210–215