Related ArticlesNMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles.
Biophys J. 2003 Oct;85(4):2589-98
Authors: Zamoon J, Mascioni A, Thomas DD, Veglia G
Phospholamban is an integral membrane protein that regulates the contractility of cardiac muscle by maintaining cardiomyocyte calcium homeostasis. Abnormalities in association of protein kinase A with PLB have recently been linked to human heart failure, where a single mutation is responsible for dilated cardiomyopathy. To date, a high-resolution structure of phospholamban in a lipid environment has been elusive. Here, we describe the first structure of recombinant, monomeric, biologically active phospholamban in lipid-mimicking dodecylphosphocholine micelles as determined by multidimensional NMR experiments. The overall structure of phospholamban is "L-shaped" with the hydrophobic domain approximately perpendicular to the cytoplasmic portion. This is in agreement with our previously published solid-state NMR data. In addition, there are two striking discrepancies between our structure and those reported previously for synthetic phospholamban in organic solvents: a), in our structure, the orientation of the cytoplasmic helix is consistent with the amphipathic nature of these residues; and b), within the hydrophobic helix, residues are positioned on two discrete faces of the helix as consistent with their functional roles ascribed by mutagenesis. This topology renders the two phosphorylation sites, Ser-16 and Thr-17, more accessible to kinases.
Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method [Biophysics and Computational Biology]
Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method
Verardi, R., Shi, L., Traaseth, N. J., Walsh, N., Veglia, G....
Date: 2011-05-31
Phospholamban (PLN) is a type II membrane protein that inhibits the sarcoplasmic reticulum Ca2+-ATPase (SERCA), thereby regulating calcium homeostasis in cardiac muscle. In membranes, PLN forms pentamers that have been proposed to function either as a storage for active monomers or as ion channels. Here, we report the T-state structure of pentameric PLN solved by a hybrid solution and...
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Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method.
Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method.
Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method.
Proc Natl Acad Sci U S A. 2011 May 16;
Authors: Verardi R, Shi L, Traaseth NJ, Walsh N, Veglia G
Phospholamban (PLN) is a type II membrane protein that inhibits the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA), thereby regulating calcium homeostasis in cardiac muscle. In membranes, PLN forms pentamers that have been proposed...
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05-19-2011 04:20 AM
[NMR paper] NMR solution structure of the monomeric form of the bacteriophage lambda capsid stabi
NMR solution structure of the monomeric form of the bacteriophage lambda capsid stabilizing protein gpD.
Related Articles NMR solution structure of the monomeric form of the bacteriophage lambda capsid stabilizing protein gpD.
J Biomol NMR. 2005 Apr;31(4):351-6
Authors: Iwai H, Forrer P, Plückthun A, Güntert P
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[NMR paper] Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge
Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate.
Related Articles Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate.
J Biol Chem. 2002 Apr 5;277(14):12375-81
Authors: Odaert B, Landrieu I, Dijkstra K, Schuurman-Wolters G, Casteels P, Wieruszeski JM, Inze D, Scheek R, Lippens G
Cyclin-dependent kinase subunit (CKS) proteins bind to cyclin-dependent...
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11-24-2010 08:49 PM
[NMR paper] The secondary structure of phospholamban: a two-dimensional NMR study.
The secondary structure of phospholamban: a two-dimensional NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The secondary structure of phospholamban: a two-dimensional NMR study.
Biochem Biophys Res Commun. 1995 Dec 26;217(3):1200-7
Authors: Maslennikov IV, Sobol AG, Anagli J, James P, Vorherr T, Arseniev AS, Carafoli E
Phospholamban (PLN) is an intrinsic membrane protein of 52 amino acids which regulates the Ca2+ pump of the sarcoplasmic reticulum of heart,...
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08-22-2010 03:50 AM
[NMR paper] Recognition of DNA by GAL4 in solution: use of a monomeric protein-DNA complex for st
Recognition of DNA by GAL4 in solution: use of a monomeric protein-DNA complex for study by NMR.
Related Articles Recognition of DNA by GAL4 in solution: use of a monomeric protein-DNA complex for study by NMR.
Biochemistry. 1994 Mar 15;33(10):3071-8
Authors: Baleja JD, Mau T, Wagner G
The complex of a monomer of GAL4 with DNA has been investigated by two-dimensional 1H nuclear magnetic resonance (NMR) spectroscopy. Previous X-ray analysis has revealed a structure in which a dimer of the N-terminal 65-residue fragment of GAL4 forms a complex,...
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[NMR paper] Recognition of DNA by GAL4 in solution: use of a monomeric protein-DNA complex for st
Recognition of DNA by GAL4 in solution: use of a monomeric protein-DNA complex for study by NMR.
Related Articles Recognition of DNA by GAL4 in solution: use of a monomeric protein-DNA complex for study by NMR.
Biochemistry. 1994 Mar 15;33(10):3071-8
Authors: Baleja JD, Mau T, Wagner G
The complex of a monomer of GAL4 with DNA has been investigated by two-dimensional 1H nuclear magnetic resonance (NMR) spectroscopy. Previous X-ray analysis has revealed a structure in which a dimer of the N-terminal 65-residue fragment of GAL4 forms a complex,...
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08-22-2010 03:33 AM
[NMR paper] Solution structure and orientation of the transmembrane anchor domain of the HIV-1-en
Solution structure and orientation of the transmembrane anchor domain of the HIV-1-encoded virus protein U by high-resolution and solid-state NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure and orientation of the transmembrane anchor domain of the HIV-1-encoded virus protein U by high-resolution and solid-state NMR spectroscopy.
Biochemistry. 1999 Apr 20;38(16):5272-82
Authors: Wray V, Kinder R, Federau T, Henklein P, Bechinger B, Schubert U
The...