ArticleBiochimica et biophysica acta2007
Structural constraints on the transmembrane and juxtamembrane regions of the phospholamban pentamer in membrane bilayers: Gln29 and Leu52.
Article in Biochimica et biophysica acta, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 16 citations in OpenAlex.
- Integrating NMR Restraints into Coarse-Grained Simulations: Toward Accurate Conformational Ensembles of Complex Protein Systems.Journal of the American Chemical Society · 2026Article
- Three Decades of REDOR in Protein Science: A Solid-State NMR Technique for Distance Measurement and Spectral Editing.International journal of molecular sciences · 2023Review
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- Article
- Accurate Determination of Conformational Transitions in Oligomeric Membrane Proteins.Scientific reports · 2016Article
- Solid state NMR and protein-protein interactions in membranes.Current opinion in structural biology · 2013Review
- Determining α-helical and β-sheet secondary structures via pulsed electron spin resonance spectroscopy.Biochemistry · 2012Article
- Isotope labeling for solution and solid-state NMR spectroscopy of membrane proteins.Advances in experimental medicine and biology · 2012Review
- Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- (15)N Solid-state NMR spectroscopic studies on phospholamban at its phosphorylated form at ser-16 in aligned phospholipid bilayers.Biochimica et biophysica acta · 2010Article
- On the function of pentameric phospholamban: ion channel or storage form?Biophysical journal · 2009Article
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4 authors at 2 institutions in 2 countries.
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Abstract
The Ca2+-ATPase of cardiac muscle cells transports Ca2+ ions against a concentration gradient into the sarcoplasmic reticulum and is regulated by phospholamban, a 52-residue integral membrane protein. It is known that phospholamban inhibits the Ca2+ pump during muscle contraction and that inhibition is removed by phosphorylation of the protein during muscle relaxation. Phospholamban forms a pentameric complex with a central pore. The solid-state magic angle spinning (MAS) NMR measurements presented here address the structure of the phospholamban pentamer in the region of Gln22-Gln29. Rotational echo double resonance (REDOR) NMR measurements show that the side chain amide groups of Gln29 are in close proximity, consistent with a hydrogen-bonded network within the central pore. 13C MAS NMR measurements are also presented on phospholamban that is 1-13C-labeled at Leu52, the last residue of the protein. pH titration of the C-terminal carboxyl group suggests that it forms a ring of negative charge on the lumenal side of the sarcoplasmic reticulum membrane. The structural constraints on the phospholamban pentamer described in this study are discussed in the context of a multifaceted mechanism for Ca2+ regulation that may involve phospholamban as both an inhibitor of the Ca2+ ATPase and as an ion channel.
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