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Solid-state 2H and 15N NMR studies of side-chain and backbone dynamics of phospholamban in lipid bilayers: Investigation of the N27A mutation
- Source :
- Biochimica et Biophysica Acta (BBA) - Biomembranes. 1798(2):210-215
- Publication Year :
- 2010
- Publisher :
- Elsevier BV, 2010.
-
Abstract
- Phospholamban (PLB) is an integral membrane protein regulating Ca(2+) 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 Ca(2+) and of cardiac contractility in vivo. The effects of this N27A mutation on the side-chain and backbone dynamics of PLB were investigated with (2)H and (15)N solid-state NMR spectroscopy in phospholipid multilamellar vesicles (MLVs). (2)H and (15)N 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 CD(3)-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 Ca(2+)-ATPase; thus, showing increased inhibition of Ca(2+)-ATPase.
- Subjects :
- SERCA
Mutation, Missense
Biophysics
Biology
010402 general chemistry
01 natural sciences
Solid-state NMR
Biochemistry
Protein Structure, Secondary
Article
Sarcoplasmic Reticulum Calcium-Transporting ATPases
03 medical and health sciences
chemistry.chemical_compound
Animals
Humans
Lipid bilayer
Integral membrane protein
POPC
Nuclear Magnetic Resonance, Biomolecular
030304 developmental biology
Phospholamban
0303 health sciences
Phospholipid membrane
Calcium-Binding Proteins
Nuclear magnetic resonance spectroscopy
Cell Biology
Transmembrane protein
0104 chemical sciences
Dynamics
Protein Structure, Tertiary
Calcium ATPase
chemistry
Amino Acid Substitution
cardiovascular system
Subjects
Details
- ISSN :
- 00052736
- Volume :
- 1798
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Biochimica et Biophysica Acta (BBA) - Biomembranes
- Accession number :
- edsair.doi.dedup.....88305d7e8aa432d40b83c4b959675da2
- Full Text :
- https://doi.org/10.1016/j.bbamem.2009.09.025