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Volumn 87, Issue 2, 2004, Pages 1205-1214

1H/15N heteronuclear NMR spectroscopy shows four dynamic domains for phospholamban reconstituted in dodecylphosphocholine micelles

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CYCLIC AMP DEPENDENT PROTEIN KINASE; DODECYLPHOSPHORYLCHOLINE; MEMBRANE PROTEIN; PHOSPHOLAMBAN; PHOSPHOPROTEIN PHOSPHATASE 1;

EID: 4143073485     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.103.038844     Document Type: Article
Times cited : (68)

References (55)
  • 1
    • 0031577283 scopus 로고    scopus 로고
    • fd coat protein structure in membrane environments: Structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix
    • Almeida, F. C. L., and S. J. Opella. 1997. fd coat protein structure in membrane environments: Structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix. J. Mol. Biol. 270:481-495.
    • (1997) J. Mol. Biol. , vol.270 , pp. 481-495
    • Almeida, F.C.L.1    Opella, S.J.2
  • 3
    • 0029029566 scopus 로고
    • Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling
    • Bruschweiler, R., X. Liao, and P. E. Wright. 1995. Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling. Science. 268:886-889.
    • (1995) Science , vol.268 , pp. 886-889
    • Bruschweiler, R.1    Liao, X.2    Wright, P.E.3
  • 4
    • 0042069902 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of recombinant Ca-ATPase regulators for high-resolution solution and solid-state NMR studies
    • Buck, B., J. Zamoon, T. Kirby, T. M. Da Silva, D. D. Thomas, and G. Veglia. 2003. Overexpression, purification, and characterization of recombinant Ca-ATPase regulators for high-resolution solution and solid-state NMR studies. Protein Express Purif. 30:253-261.
    • (2003) Protein Express Purif. , vol.30 , pp. 253-261
    • Buck, B.1    Zamoon, J.2    Kirby, T.3    Da Silva, T.M.4    Thomas, D.D.5    Veglia, G.6
  • 5
    • 0033543151 scopus 로고    scopus 로고
    • Backbone dynamics of the N-terminal domain of the HIV-1 capsid protein and comparison with the G94D mutant conferring cyclosporin resistance/dependence
    • Campos-Olivas, R., and M. F. Summers. 1999. Backbone dynamics of the N-terminal domain of the HIV-1 capsid protein and comparison with the G94D mutant conferring cyclosporin resistance/dependence. Biochemistry. 38:10262-10271.
    • (1999) Biochemistry , vol.38 , pp. 10262-10271
    • Campos-Olivas, R.1    Summers, M.F.2
  • 6
    • 33847534249 scopus 로고
    • Effects of diffusion on free precession in nuclear magnetic resonance experiments
    • Carr, H. Y., and E. M. Purcell. 1954. Effects of diffusion on free precession in nuclear magnetic resonance experiments. Phys. Rev. 94:630-638.
    • (1954) Phys. Rev. , vol.94 , pp. 630-638
    • Carr, H.Y.1    Purcell, E.M.2
  • 7
    • 0036947172 scopus 로고    scopus 로고
    • From mouse to man: Understanding heart failure through genetically altered mouse models
    • Chu, G., K. Haghighi, and E. G. Kranias. 2002. From mouse to man: understanding heart failure through genetically altered mouse models. J. Card. Fail. 8(Suppl):S432-S449.
    • (2002) J. Card. Fail. , vol.8 , Issue.SUPPL.
    • Chu, G.1    Haghighi, K.2    Kranias, E.G.3
  • 9
    • 85030818502 scopus 로고    scopus 로고
    • Defining the membrane delimitation of phospholamban
    • Abstr.
    • Cornea, R. L., Z. Chen, and L. R. Jones. 2002. Defining the membrane delimitation of phospholamban. Biophys. J. 82:227a, (Abstr.)
    • (2002) Biophys. J. , vol.82
    • Cornea, R.L.1    Chen, Z.2    Jones, L.R.3
  • 10
    • 0030978470 scopus 로고    scopus 로고
    • Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers
    • Cornea, R. L., L. R. Jones, J. M. Autry, and D. D. Thomas. 1997. Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers. Biochemistry. 36:2960-2967.
    • (1997) Biochemistry , vol.36 , pp. 2960-2967
    • Cornea, R.L.1    Jones, L.R.2    Autry, J.M.3    Thomas, D.D.4
  • 11
  • 12
    • 0033546403 scopus 로고    scopus 로고
    • Backbone dynamics and energetics of a calmodulin domain mutant exchanging between closed and open conformations
    • Evenäs, J., S. Forsén, A. Malmendal, and M. Akke. 1999. Backbone dynamics and energetics of a calmodulin domain mutant exchanging between closed and open conformations. J. Mol. Biol. 289:603-617.
    • (1999) J. Mol. Biol. , vol.289 , pp. 603-617
    • Evenäs, J.1    Forsén, S.2    Malmendal, A.3    Akke, M.4
  • 14
    • 0023119953 scopus 로고
    • Complete complementary DNA-derived amino acid sequence of canine cardiac phospholamban
    • Fujii, J., A. Ueno, K. Kitano, S. Tanaka, M. Kadoma, and M. Tada. 1987. Complete complementary DNA-derived amino acid sequence of canine cardiac phospholamban. J. Clin. Invest. 79:301-304.
    • (1987) J. Clin. Invest. , vol.79 , pp. 301-304
    • Fujii, J.1    Ueno, A.2    Kitano, K.3    Tanaka, S.4    Kadoma, M.5    Tada, M.6
  • 16
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Johnson, B. A., and R. A. Blevins. 1994. NMRView: A computer program for the visualization and analysis of NMR data. J. Biomol. NMR. 4:603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 19
    • 0034609576 scopus 로고    scopus 로고
    • Synthetic null-cysteine phospholamban analogue and the corresponding transmembrane domain inhibit the Ca-ATPase
    • Karim, C. B., C. G. Marquardt, J. D. Stamm, G. Barany, and D. D. Thomas. 2000. Synthetic null-cysteine phospholamban analogue and the corresponding transmembrane domain inhibit the Ca-ATPase. Biochemistry. 39:10892-10897.
    • (2000) Biochemistry , vol.39 , pp. 10892-10897
    • Karim, C.B.1    Marquardt, C.G.2    Stamm, J.D.3    Barany, G.4    Thomas, D.D.5
  • 20
    • 0032168447 scopus 로고    scopus 로고
    • Cysteine reactivity and oligomeric structures of phospholamban and its mutants
    • Karim, C. B., J. D. Stamm, J. Karim, L. R. Jones, and D. D. Thomas. 1998. Cysteine reactivity and oligomeric structures of phospholamban and its mutants. Biochemistry. 37:12074-12081.
    • (1998) Biochemistry , vol.37 , pp. 12074-12081
    • Karim, C.B.1    Stamm, J.D.2    Karim, J.3    Jones, L.R.4    Thomas, D.D.5
  • 21
    • 0030989981 scopus 로고    scopus 로고
    • Phospholamban inhibitory function is activated by depolymerization
    • Kimura, Y., K. Kurzydlowski, M. Tada, and D. H. MacLennan. 1997. Phospholamban inhibitory function is activated by depolymerization. J. Biol. Chem. 272:15061-15064.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15061-15064
    • Kimura, Y.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 22
    • 2442553272 scopus 로고    scopus 로고
    • EPR reveals a large-scale conformational change in the cytoplasmic domain of PLB upon binding to the SR CaATPase
    • Kirby, T. L., C. B. Karim, and D. D. Thomas. 2004. EPR reveals a large-scale conformational change in the cytoplasmic domain of PLB upon binding to the SR CaATPase. Biochemistry. 43:5842-5852.
    • (2004) Biochemistry , vol.43 , pp. 5842-5852
    • Kirby, T.L.1    Karim, C.B.2    Thomas, D.D.3
  • 24
    • 0041817968 scopus 로고    scopus 로고
    • Phosphorylation by cAMP-dependent protein kinase modulates the structural coupling between the transmembrane and cytosolic domains of phospholamban
    • Li, J., D. J. Bigelow, and T. C. Squire. 2003. Phosphorylation by cAMP-dependent protein kinase modulates the structural coupling between the transmembrane and cytosolic domains of phospholamban. Biochemistry. 36:10674-10682.
    • (2003) Biochemistry , vol.36 , pp. 10674-10682
    • Li, J.1    Bigelow, D.J.2    Squire, T.C.3
  • 25
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari, G., and A. Szabo. 1982a. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104:4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 26
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results
    • Lipari, G., and A. Szabo. 1982b. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results. J. Am. Chem. Soc. 104:4559-4570.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 27
    • 0038464639 scopus 로고    scopus 로고
    • Phospholamban: A crucial regulator of cardiac contractility
    • MacLennan, D. H., and E. G. Kranias. 2003. Phospholamban: a crucial regulator of cardiac contractility. Nat. Rev. Mol. Cell Biol. 4:566-578.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 566-578
    • MacLennan, D.H.1    Kranias, E.G.2
  • 28
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease H1: Correlations with structure and function in an active enzyme
    • Mandel, A. M., M. Akke, and A. G. Palmer. 1995. Backbone dynamics of Escherichia coli ribonuclease H1: Correlations with structure and function in an active enzyme. J. Mol. Biol. 246:144-163.
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 29
    • 0037077536 scopus 로고    scopus 로고
    • Solid-state NMR and rigid body molecular dynamics to determine domain orientations of monomeric phospholamban
    • Mascioni, A., C. Karim, J. Zamoon, D. D. Thomas, and G. Veglia. 2002. Solid-state NMR and rigid body molecular dynamics to determine domain orientations of monomeric phospholamban. J. Am. Chem. Soc.124:9392-9393.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9392-9393
    • Mascioni, A.1    Karim, C.2    Zamoon, J.3    Thomas, D.D.4    Veglia, G.5
  • 30
    • 0002899752 scopus 로고
    • Modified spin-echo method for measuring nuclear relaxation times
    • Meiboom, S., and D. Gill. 1958. Modified spin-echo method for measuring nuclear relaxation times. Rev. Sci. Instr. 29:688-691.
    • (1958) Rev. Sci. Instr. , vol.29 , pp. 688-691
    • Meiboom, S.1    Gill, D.2
  • 31
    • 0035072684 scopus 로고    scopus 로고
    • Anisotropic rotational diffusion in model-free analysis for a ternary DHFR complex
    • Osborne, M. J., and P. E. Wright. 2001. Anisotropic rotational diffusion in model-free analysis for a ternary DHFR complex. J. Biomol. NMR. 19:209-230.
    • (2001) J. Biomol. NMR , vol.19 , pp. 209-230
    • Osborne, M.J.1    Wright, P.E.2
  • 32
    • 0028329918 scopus 로고
    • Release of peptides and proteins from fusion proteins using a recombinant plant virus proteinase
    • Parks, T. D., K. K. Leuther, E. D. Howard, S. A. Johnson, and W. G. Dougherty. 1994. Release of peptides and proteins from fusion proteins using a recombinant plant virus proteinase. Anal. Biochem. 216:413-417.
    • (1994) Anal. Biochem. , vol.216 , pp. 413-417
    • Parks, T.D.1    Leuther, K.K.2    Howard, E.D.3    Johnson, S.A.4    Dougherty, W.G.5
  • 33
    • 0034919305 scopus 로고    scopus 로고
    • NMR methods for quantifying microsecond-to-millisecond motions in biological macromolecules
    • Palmer, A. G., 3rd, C. D. Kroenke, and J. P. Loria. 2001. NMR methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol. 339:204-238.
    • (2001) Methods Enzymol. , vol.339 , pp. 204-238
    • Palmer III, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 35
    • 0000486802 scopus 로고
    • Suppression of the effects of cross-relaxation between dipolar and anisotropic chemical shift relaxation mechanisms in the measurements of spin-spin relaxation rates
    • Palmer, A. G. 3rd, N. J. Skelton, W. J. Chazin, P. E. Wright, and M. Rance. 1992. Suppression of the effects of cross-relaxation between dipolar and anisotropic chemical shift relaxation mechanisms in the measurements of spin-spin relaxation rates. Mol. Phys. 75:699-711.
    • (1992) Mol. Phys. , vol.75 , pp. 699-711
    • Palmer III, A.G.1    Skelton, N.J.2    Chazin, W.J.3    Wright, P.E.4    Rance, M.5
  • 37
    • 0001610304 scopus 로고
    • Notes on bias in estimation
    • Quenouille, M. H. 1956. Notes on bias in estimation. Biometrika. 43:353-360.
    • (1956) Biometrika , vol.43 , pp. 353-360
    • Quenouille, M.H.1
  • 38
    • 0033616627 scopus 로고    scopus 로고
    • Depolymerization of phospholamban in the presence of calcium pump: A fluorescence energy transfer study
    • Reddy, L. G., L. R. Jones, and D. D. Thomas. 1999. Depolymerization of phospholamban in the presence of calcium pump: a fluorescence energy transfer study. Biochemistry. 38:3954-3962.
    • (1999) Biochemistry , vol.38 , pp. 3954-3962
    • Reddy, L.G.1    Jones, L.R.2    Thomas, D.D.3
  • 40
    • 0028541223 scopus 로고
    • A test of the model free formulas. Effects of anisotropic rotational diffusion and dimerization
    • Schurr, J. M., H. P. Babcock, and B. Fujimoto. 1994. A test of the model free formulas. Effects of anisotropic rotational diffusion and dimerization. J. Magn. Reson. B. 105:211-224.
    • (1994) J. Magn. Reson. B , vol.105 , pp. 211-224
    • Schurr, J.M.1    Babcock, H.P.2    Fujimoto, B.3
  • 41
    • 13444269041 scopus 로고
    • Computer-optimized decoupling scheme for wideband applications and low-level operation
    • Shaka, A. J., P. B. Barker, and R. Freeman. 1985. Computer-optimized decoupling scheme for wideband applications and low-level operation. J. Magn. Reson. 64:547-552.
    • (1985) J. Magn. Reson. , vol.64 , pp. 547-552
    • Shaka, A.J.1    Barker, P.B.2    Freeman, R.3
  • 42
    • 0031722958 scopus 로고    scopus 로고
    • Phospholamban: Protein structure, mechanism of action, and role in cardiac function
    • Simmerman, H. K., and L. R. Jones. 1998. Phospholamban: protein structure, mechanism of action, and role in cardiac function. Physiol. Rev. 78:921-947.
    • (1998) Physiol. Rev. , vol.78 , pp. 921-947
    • Simmerman, H.K.1    Jones, L.R.2
  • 45
    • 0024669188 scopus 로고
    • Regulation of the Ca2+ pump ATPase by cAMP-dependent phosphorylation of phospholamban
    • Tada, M., and M. Kadoma. 1989. Regulation of the Ca2+ pump ATPase by cAMP-dependent phosphorylation of phospholamban. Bioessays. 10:157-163.
    • (1989) Bioessays , vol.10 , pp. 157-163
    • Tada, M.1    Kadoma, M.2
  • 46
    • 0031736237 scopus 로고    scopus 로고
    • Direct spectroscopic detection of molecular dynamics and interactions of the calcium pump and phospholamban
    • Thomas, D. D., L. G. Reddy, C. B. Karim, M. Li, R. Cornea, J. M. Autry, L. R. Jones, and J. Stamm. 1998. Direct spectroscopic detection of molecular dynamics and interactions of the calcium pump and phospholamban. Ann. N. Y. Acad. Sci. 853:186-194.
    • (1998) Ann. N. Y. Acad. Sci. , vol.853 , pp. 186-194
    • Thomas, D.D.1    Reddy, L.G.2    Karim, C.B.3    Li, M.4    Cornea, R.5    Autry, J.M.6    Jones, L.R.7    Stamm, J.8
  • 49
    • 0029900275 scopus 로고    scopus 로고
    • 15N chemical shift anisotropy from quantitative measurement of relaxation interference effects
    • 15N chemical shift anisotropy from quantitative measurement of relaxation interference effects. J. Am. Chem. Soc. 118:6986-6991.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6986-6991
    • Tjandra, N.1    Szabo, A.2    Bax, A.3
  • 51
    • 0036217488 scopus 로고    scopus 로고
    • Deuterium/hydrogen exchange factors measured by solution nuclear magnetic resonance spectroscopy as indicators of the structure and topology of membrane proteins
    • Veglia, G., A. C. Zeri, C. Ma, and S. J. Opella. 2002. Deuterium/hydrogen exchange factors measured by solution nuclear magnetic resonance spectroscopy as indicators of the structure and topology of membrane proteins. Biophys. J. 82:2176-2183.
    • (2002) Biophys. J. , vol.82 , pp. 2176-2183
    • Veglia, G.1    Zeri, A.C.2    Ma, C.3    Opella, S.J.4
  • 53
    • 0029996040 scopus 로고    scopus 로고
    • Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by solution NMR
    • Williams, K. A., N. A. Farrow, C. M. Deber, and L. E. Kay. 1996. Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by solution NMR. Biochemistry. 35:5145-5157.
    • (1996) Biochemistry , vol.35 , pp. 5145-5157
    • Williams, K.A.1    Farrow, N.A.2    Deber, C.M.3    Kay, L.E.4
  • 55
    • 0141530952 scopus 로고    scopus 로고
    • NMR solution structure and topological orientation of monomeric pho spholamban in dodecylphosphocholine micelles
    • Zamoon, J., A. Mascioni, D. D. Thomas, and G. Veglia. 2003. NMR solution structure and topological orientation of monomeric pho spholamban in dodecylphosphocholine micelles. Biophys. J. 85:2589-2598.
    • (2003) Biophys. J. , vol.85 , pp. 2589-2598
    • Zamoon, J.1    Mascioni, A.2    Thomas, D.D.3    Veglia, G.4


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