ArticleBiophysical journal2004
(1)H/(15)N heteronuclear NMR spectroscopy shows four dynamic domains for phospholamban reconstituted in dodecylphosphocholine micelles.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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40 citing papers in PubMed, 83 citations in OpenAlex.
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- Structure, self-assembly, and properties of a truncated reflectin variant.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- NMR Structure of the FIV gp36 C-Terminal Heptad Repeat and Membrane-Proximal External Region.International journal of molecular sciences · 2020Article
- Effect of Phosphorylation on Interactions between Transmembrane Domains of SERCA and Phospholamban.Biophysical journal · 2018Article
- Effects of the Arg9Cys and Arg25Cys mutations on phospholamban's conformational equilibrium in membrane bilayers.Biochimica et biophysica acta. Biomembranes · 2018Article
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- Phospholamban phosphorylation, mutation, and structural dynamics: a biophysical approach to understanding and treating cardiomyopathy.Biophysical reviews · 2015Article
- Effects of naturally occurring arginine 14 deletion on phospholamban conformational dynamics and membrane interactions.Biochimica et biophysica acta · 2015Article
- Mapping membrane protein backbone dynamics: a comparison of site-directed spin labeling with NMR 15N-relaxation measurements.Biophysical journal · 2014Article
- Structural dynamics and topology of phosphorylated phospholamban homopentamer reveal its role in the regulation of calcium transport.Structure (London, England : 1993) · 2013Article
- Structures of the excited states of phospholamban and shifts in their populations upon phosphorylation.Biochemistry · 2013Article
- Tuning the structural coupling between the transmembrane and cytoplasmic domains of phospholamban to control sarcoplasmic reticulum Ca(2+)-ATPase (SERCA) function.Journal of muscle research and cell motility · 2012Article
- Structural and functional dynamics of an integral membrane protein complex modulated by lipid headgroup charge.Journal of molecular biology · 2012Article
- Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.Biochimica et biophysica acta · 2012Article
- cAMP-dependent protein kinase A selects the excited state of the membrane substrate phospholamban.Journal of molecular biology · 2011Article
- Gramicidin A backbone and side chain dynamics evaluated by molecular dynamics simulations and nuclear magnetic resonance experiments. II: nuclear magnetic resonance experiments.The journal of physical chemistry. B · 2011Article
- 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
- Lipid-mediated folding/unfolding of phospholamban as a regulatory mechanism for the sarcoplasmic reticulum Ca2+-ATPase.Journal of molecular biology · 2011Article
- An allosteric mechanism inferred from molecular dynamics simulations on phospholamban pentamer in lipid membranes.PloS one · 2011Article
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4 authors at 1 institution in 1 country.
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Abstract
We report the backbone dynamics of monomeric phospholamban in dodecylphosphocholine micelles using (1)H/(15)N heteronuclear NMR spectroscopy. Phospholamban is a 52-amino acid membrane protein that regulates Ca-ATPase in cardiac muscle. Phospholamban comprises three structural domains: a transmembrane domain from residues 22 to 52, a connecting loop from 17 to 21, and a cytoplasmic domain from 1 to 16 that is organized in an "L"-shaped structure where the transmembrane and the cytoplasmic domain form an angle of approximately 80 degrees (Zamoon et al., 2003; Mascioni et al., 2002). T(1), T(2), and (1)H/(15)N nuclear Overhauser effect values measured for the amide backbone resonances were interpreted using the model-free approach of Lipari and Szabo. The results point to the existence of four dynamic domains, revealing the overall plasticity of the cytoplasmic helix, the flexible loop, and part of the transmembrane domain (residues 22-30). In addition, using Carr-Purcell-Meiboom-Gill-based experiments, we have characterized phospholamban dynamics in the micros-ms timescale. We found that the majority of the residues in the cytoplasmic domain, the flexible loop, and the first ten residues of the transmembrane domain undergo dynamics in the micros-ms range, whereas minimal dynamics were detected for the transmembrane domain. Hydrogen/deuterium exchange factors measured at different temperatures support the existence of slow motion in both the loop and the cytoplasmic helix. We propose that these dynamic properties are critical factors in the biomolecular recognition of phospholamban by Ca-ATPase and other interacting proteins such as protein kinase A and protein phosphatase 1.
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