Related ArticlesConformation of the cytoplasmic domain of phospholamban by NMR and CD.
Mol Membr Biol. 1994 Oct-Dec;11(4):263-9
Authors: Hubbard JA, MacLachlan LK, Meenan E, Salter CJ, Reid DG, Lahouratate P, Humphries J, Stevens N, Bell D, Neville WA
Nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy have been used to characterize the conformation of the putative cytoplasmic domain of phospholamban (PLB), an oligomeric membrane-bound protein which regulates the activity of the cardiac sarcoplasmic reticulum Ca(2+)-dependent ATPase. In aqueous solution the 25-residue peptide adopts a number of rapidly interconverting conformers with no secondary structural type obviously predominating. However, in trifluoroethanol (TFE) the conformation, while still highly dynamic, is characterized by a high proportion of helical structures. Evidence for this is provided by alpha CH chemical shifts and low NH chemical shift temperature coefficients, small NH-alpha CH intraresidue scalar coupling constants, a substantial number of distinctive interresidue nuclear Overhauser effects (NOEs) [dNN(i, i + 1), d alpha N(i, i + 3), d alpha beta(i, i + 3) and d alpha N(i, i + 4)] and characteristic CD bands at 190 (positive), 206 (negative) and 222 nm (negative). The helicity is interrupted around Pro-21. The activity of PLB is regulated by phosphorylation at either Ser-16 or Thr-17. CD shows that phosphorylation at Ser-16 by the cAMP-activated protein kinase causes about an 11% decrease in alpha-helical content in TFE.
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Biomol NMR Assign. 2011 Jun 7;
Authors: Wood K, Paz A, Dijkstra K, Scheek RM, Otten R, Silman I, Sussman JL, Mulder FA
Neuroligins act as heterophilic adhesion molecules at neuronal synapses. Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered. Here we...
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06-08-2011 11:30 AM
[NMR paper] The conformation of the cytoplasmic helix 8 of the CB1 cannabinoid receptor using NMR
The conformation of the cytoplasmic helix 8 of the CB1 cannabinoid receptor using NMR and circular dichroism.
Related Articles The conformation of the cytoplasmic helix 8 of the CB1 cannabinoid receptor using NMR and circular dichroism.
Biochim Biophys Acta. 2005 Feb 1;1668(1):1-9
Authors: Choi G, Guo J, Makriyannis A
The cytoplasmic helix domain (fourth cytoplasmic loop, helix 8) of numerous GPCRs such as rhodopsin and the beta-adrenergic receptor exhibits unique structural and functional characteristics. Computational models also predict the...
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11-24-2010 11:14 PM
[NMR paper] Investigating the dynamic properties of the transmembrane segment of phospholamban in
Investigating the dynamic properties of the transmembrane segment of phospholamban incorporated into phospholipid bilayers utilizing 2H and 15N solid-state NMR spectroscopy.
Related Articles Investigating the dynamic properties of the transmembrane segment of phospholamban incorporated into phospholipid bilayers utilizing 2H and 15N solid-state NMR spectroscopy.
Biochemistry. 2004 Nov 9;43(44):13899-909
Authors: Tiburu EK, Karp ES, Dave PC, Damodaran K, Lorigan GA
(2)H and (15)N solid-state NMR spectroscopic techniques were used to investigate...
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[NMR paper] What is the average conformation of bacteriophage T4 lysozyme in solution? A domain o
What is the average conformation of bacteriophage T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMR.
Related Articles What is the average conformation of bacteriophage T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMR.
J Mol Biol. 2001 May 11;308(4):745-64
Authors: Goto NK, Skrynnikov NR, Dahlquist FW, Kay LE
Lysozyme from T4 bacteriophage is comprised of two domains that are both involved in binding substrate. Although wild-type lysozyme has...
[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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[KPWU blog] [IDP] Cytoplasmic Domain of the T Cell Receptor zeta
Cytoplasmic Domain of the T Cell Receptor zeta
Title:* The Intrinsically Disordered Cytoplasmic Domain of the T Cell Receptor ? Chain Binds to the Nef Protein of Simian Immunodeficiency Virus without a Disorder-to-Order Transition Authors: Alexander B. Sigalov, Walter M. Kim, Maria Saline and Lawrence J. Stern Journal: Biochemistry, 2008, 47 (49), pp 12942–12944 Not fully labeled in HSQChttp://stats.wordpress.com/b.gif?host=kpwu.wordpress.com&blog=76132&post=197&subd=kpwu&ref=&feed=1
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[NMR paper] Interaction of calmodulin with phospholamban and caldesmon: comparative studies by 1H
Interaction of calmodulin with phospholamban and caldesmon: comparative studies by 1H-NMR spectroscopy.
Related Articles Interaction of calmodulin with phospholamban and caldesmon: comparative studies by 1H-NMR spectroscopy.
Biochim Biophys Acta. 1992 Nov 10;1160(1):22-34
Authors: Gao Y, Levine BA, Mornet D, Slatter DA, Strasburg GM
In order to identify comparative aspects of the interaction of calmodulin with its target proteins, proton magnetic-resonance studies of complex formation between calmodulin and defined segments of phospholamban...
Conformation of the cytoplasmic domain of phospholamban by NMR and CD.
Linear Mode
