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Volumn 6, Issue 7, 2009, Pages 532-537

Mapping the structure and conformational movements of proteins with transition metal ion FRET

Author keywords

[No Author keywords available]

Indexed keywords

COPPER; CYCLIC AMP; CYCLIC NUCLEOTIDE GATED CHANNEL; CYCLIC NUCLEOTIDE GATED CHANNEL HCN2; FLUORESCENT DYE; METAL ION; NICKEL; UNCLASSIFIED DRUG;

EID: 67649604544     PISSN: 15487091     EISSN: 15491676     Source Type: Journal    
DOI: 10.1038/nmeth.1341     Document Type: Article
Times cited : (139)

References (38)
  • 1
    • 0141831003 scopus 로고    scopus 로고
    • Structural basis for modulation and agonist specificity of HCN pacemaker channels
    • Zagotta, W.N. et al. Structural basis for modulation and agonist specificity of HCN pacemaker channels. Nature 425, 200-205 (2003).
    • (2003) Nature , vol.425 , pp. 200-205
    • Zagotta, W.N.1
  • 2
    • 0028913136 scopus 로고
    • Fluorescence resonance energy transfer
    • Selvin, P.R. Fluorescence resonance energy transfer. Methods Enzymol. 246, 300-334 (1995).
    • (1995) Methods Enzymol , vol.246 , pp. 300-334
    • Selvin, P.R.1
  • 3
    • 46149091062 scopus 로고    scopus 로고
    • Extent of voltage sensor movement during gating of shaker K+ channels
    • Posson, D.J. & Selvin, P.R. Extent of voltage sensor movement during gating of shaker K+ channels. Neuron 59, 98-109 (2008).
    • (2008) Neuron , vol.59 , pp. 98-109
    • Posson, D.J.1    Selvin, P.R.2
  • 4
    • 37649015345 scopus 로고    scopus 로고
    • Effect of flexibility and cis residues in single-molecule FRET studies of polyproline
    • Best, R.B. et al. Effect of flexibility and cis residues in single-molecule FRET studies of polyproline. Proc. Natl. Acad. Sci. USA 104, 18964-18969 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 18964-18969
    • Best, R.B.1
  • 5
    • 0036085517 scopus 로고    scopus 로고
    • Principles and biophysical applications of lanthanide-based probes
    • Selvin, P.R. Principles and biophysical applications of lanthanide-based probes. Annu. Rev. Biophys. Biomol. Struct. 31, 275-302 (2002).
    • (2002) Annu. Rev. Biophys. Biomol. Struct , vol.31 , pp. 275-302
    • Selvin, P.R.1
  • 7
    • 36048946776 scopus 로고    scopus 로고
    • In vivo measurement of intramolecular distances using genetically encoded reporters
    • Sandtner, W., Bezanilla, F. & Correa, A.M. In vivo measurement of intramolecular distances using genetically encoded reporters. Biophys. J. 93, L45-L47 (2007).
    • (2007) Biophys. J , vol.93
    • Sandtner, W.1    Bezanilla, F.2    Correa, A.M.3
  • 10
    • 0025730892 scopus 로고
    • Engineered metal-binding proteins: Purification to protein folding
    • Arnold, F.H. & Haymore, B.L. Engineered metal-binding proteins: purification to protein folding. Science 252, 1796-1797 (1991).
    • (1991) Science , vol.252 , pp. 1796-1797
    • Arnold, F.H.1    Haymore, B.L.2
  • 11
    • 0025925381 scopus 로고
    • Characterization of His-X3-His sites in alpha-helices of synthetic metal-binding bovine somatotropin
    • Suh, S.S., Haymore, B.L. & Arnold, F.H. Characterization of His-X3-His sites in alpha-helices of synthetic metal-binding bovine somatotropin. Protein Eng. 4, 301-305 (1991).
    • (1991) Protein Eng , vol.4 , pp. 301-305
    • Suh, S.S.1    Haymore, B.L.2    Arnold, F.H.3
  • 12
    • 33645313112 scopus 로고    scopus 로고
    • CNG and HCN channels: Two peas, one pod
    • Craven, K.B. & Zagotta, W.N. CNG and HCN channels: Two peas, one pod. Annu. Rev. Physiol. 68, 375-401 (2006).
    • (2006) Annu. Rev. Physiol , vol.68 , pp. 375-401
    • Craven, K.B.1    Zagotta, W.N.2
  • 13
    • 0018464261 scopus 로고
    • The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer
    • Dale, R.E., Eisinger, J. & Blumberg, W.E. The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer. Biophys. J. 26, 161-193 (1979).
    • (1979) Biophys. J , vol.26 , pp. 161-193
    • Dale, R.E.1    Eisinger, J.2    Blumberg, W.E.3
  • 15
    • 84935354375 scopus 로고    scopus 로고
    • Forster, T. Experimentelle und theoretische untersuchung des zwischenmolekularen ubergangs von elektronenanregungsenergie. Zeitschrift Fur Naturforschung Section A4, 321-3271949 A 4, 321-327 (1949).
    • Forster, T. Experimentelle und theoretische untersuchung des zwischenmolekularen ubergangs von elektronenanregungsenergie. Zeitschrift Fur Naturforschung Section A4, 321-3271949 A 4, 321-327 (1949).
  • 16
    • 0018650688 scopus 로고
    • An analytic solution to the Forster energy transfer problem in two dimensions
    • Wolber, P.K. & Hudson, B.S. An analytic solution to the Forster energy transfer problem in two dimensions. Biophys. J. 28, 197-210 (1979).
    • (1979) Biophys. J , vol.28 , pp. 197-210
    • Wolber, P.K.1    Hudson, B.S.2
  • 17
    • 0028903255 scopus 로고
    • Calculation of resonance energy transfer in crowded biological membranes
    • Zimet, D.B., Thevenin, B.J., Verkman, A.S., Shohet, S.B. & Abney, J.R. Calculation of resonance energy transfer in crowded biological membranes. Biophys. J. 68, 1592-1603 (1995).
    • (1995) Biophys. J , vol.68 , pp. 1592-1603
    • Zimet, D.B.1    Thevenin, B.J.2    Verkman, A.S.3    Shohet, S.B.4    Abney, J.R.5
  • 18
    • 51049115964 scopus 로고    scopus 로고
    • FRET with multiply labeled HERG K(+) channels as a reporter of the in vivo coarse architecture of the cytoplasmic domains
    • Miranda, P. et al. FRET with multiply labeled HERG K(+) channels as a reporter of the in vivo coarse architecture of the cytoplasmic domains. Biochim. Biophys. Acta 1783, 1681-1699 (2008).
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 1681-1699
    • Miranda, P.1
  • 19
    • 34548499865 scopus 로고    scopus 로고
    • Structural dynamics in the gating ring of cyclic nucleotide-gated ion channels
    • Taraska, J.W. & Zagotta, W.N. Structural dynamics in the gating ring of cyclic nucleotide-gated ion channels. Nat. Struct. Mol. Biol. 14, 854-860 (2007).
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 854-860
    • Taraska, J.W.1    Zagotta, W.N.2
  • 20
    • 14744283294 scopus 로고
    • Protein stabilization by engineered metal chelation
    • Kellis, J.T. Jr., Todd, R.J. & Arnold, F.H. Protein stabilization by engineered metal chelation. Bio/Technology 9, 994-995 (1991).
    • (1991) Bio/Technology , vol.9 , pp. 994-995
    • Kellis Jr., J.T.1    Todd, R.J.2    Arnold, F.H.3
  • 21
    • 0025753633 scopus 로고
    • Cu(II)-binding properties of a cytochrome c with a synthetic metal-binding site: His-X3-His in an alpha-helix
    • Todd, R.J., Van Dam, M.E., Casimiro, D., Haymore, B.L. & Arnold, F.H. Cu(II)-binding properties of a cytochrome c with a synthetic metal-binding site: His-X3-His in an alpha-helix. Proteins 10 156-161 (1991).
    • (1991) Proteins , vol.10 , pp. 156-161
    • Todd, R.J.1    Van Dam, M.E.2    Casimiro, D.3    Haymore, B.L.4    Arnold, F.H.5
  • 22
    • 33845800991 scopus 로고    scopus 로고
    • Capturing cyclic nucleotides in action: Snapshots from crystallographic studies
    • Rehmann, H., Wittinghofer, A. & Bos, J.L. Capturing cyclic nucleotides in action: Snapshots from crystallographic studies. Nat. Rev. Mol. Cell Biol. 8, 63-73 (2007).
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 63-73
    • Rehmann, H.1    Wittinghofer, A.2    Bos, J.L.3
  • 23
    • 47849110347 scopus 로고    scopus 로고
    • Structural and energetic analysis of activation by a cyclic nucleotide binding domain
    • Altieri, S.L. et al. Structural and energetic analysis of activation by a cyclic nucleotide binding domain. J. Mol. Biol. 381, 655-669 (2008).
    • (2008) J. Mol. Biol , vol.381 , pp. 655-669
    • Altieri, S.L.1
  • 24
    • 13244291292 scopus 로고    scopus 로고
    • Crystal structure of a complex between the catalytic and regulatory (RIalpha) subunits of PKA
    • Kim, C., Xuong, N.H. & Taylor, S.S. Crystal structure of a complex between the catalytic and regulatory (RIalpha) subunits of PKA. Science 307, 690-696 (2005).
    • (2005) Science , vol.307 , pp. 690-696
    • Kim, C.1    Xuong, N.H.2    Taylor, S.S.3
  • 25
    • 31844447089 scopus 로고    scopus 로고
    • Structure of the cyclic-AMP-responsive exchange factor Epac2 in its auto-inhibited state
    • Rehmann, H., Das, J., Knipscheer, P., Wittinghofer, A. & Bos, J.L. Structure of the cyclic-AMP-responsive exchange factor Epac2 in its auto-inhibited state. Nature 439, 625-628 (2006).
    • (2006) Nature , vol.439 , pp. 625-628
    • Rehmann, H.1    Das, J.2    Knipscheer, P.3    Wittinghofer, A.4    Bos, J.L.5
  • 26
    • 0000199497 scopus 로고
    • Energy transfer between terbium (III) and cobalt (II) in thermolysin: A new class of metal-metal distance probes
    • Horrocks, W.D. Jr., Holmquist, B. & Vallee, B.L. Energy transfer between terbium (III) and cobalt (II) in thermolysin: A new class of metal-metal distance probes. Proc. Natl. Acad. Sci. USA 72, 4764-4768 (1975).
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 4764-4768
    • Horrocks Jr., W.D.1    Holmquist, B.2    Vallee, B.L.3
  • 27
    • 34249896932 scopus 로고    scopus 로고
    • Structure and rearrangements in the carboxy-terminal region of SpIH channels
    • Flynn, G.E., Black, K.D., Islas, L.D., Sankaran, B. & Zagotta, W.N. Structure and rearrangements in the carboxy-terminal region of SpIH channels. Structure 15, 671-682 (2007).
    • (2007) Structure , vol.15 , pp. 671-682
    • Flynn, G.E.1    Black, K.D.2    Islas, L.D.3    Sankaran, B.4    Zagotta, W.N.5
  • 28
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy, A.J. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr. D Biol. Crystallogr. 63, 32-41 (2007).
    • (2007) Acta Crystallogr. D Biol. Crystallogr , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 29
    • 84920325457 scopus 로고
    • AMoRe - an automated package for molecular replacement
    • Navaza, J. AMoRe - an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 30
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 31
  • 33
    • 0001897686 scopus 로고
    • Assessment of phase accuracy by cross validation - the free R-value - methods and applications
    • Brunger, A.T. Assessment of phase accuracy by cross validation - the free R-value - methods and applications. Acta Crystallogr. D Biol. Crystallogr. 49, 24-36 (1993).
    • (1993) Acta Crystallogr. D Biol. Crystallogr , vol.49 , pp. 24-36
    • Brunger, A.T.1
  • 34
    • 0028103275 scopus 로고    scopus 로고
    • The C.C.P. 4 suite: Programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994).
    • The C.C.P. 4 suite: Programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994).
  • 35
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A.T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D Biol. Crystallogr , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 36
    • 0141841775 scopus 로고    scopus 로고
    • Crystal structure of the nickel-responsive transcription factor NikR
    • Schreiter, E.R. et al. Crystal structure of the nickel-responsive transcription factor NikR. Nat. Struct. Biol. 10, 794-799 (2003).
    • (2003) Nat. Struct. Biol , vol.10 , pp. 794-799
    • Schreiter, E.R.1
  • 37
    • 28444469196 scopus 로고    scopus 로고
    • Structural studies of an engineered zinc biosensor reveal an unanticipated mode of zinc binding
    • Telmer, P.G. & Shilton, B.H. Structural studies of an engineered zinc biosensor reveal an unanticipated mode of zinc binding. J. Mol. Biol. 354, 829-840 (2005).
    • (2005) J. Mol. Biol , vol.354 , pp. 829-840
    • Telmer, P.G.1    Shilton, B.H.2
  • 38
    • 0034038551 scopus 로고    scopus 로고
    • Use of a non-rigid region in T4 lysozyme to design an adaptable metal-binding site
    • Wray, J.W., Baase, W.A., Ostheimer, G.J., Zhang, X.J. & Matthews, B.W. Use of a non-rigid region in T4 lysozyme to design an adaptable metal-binding site. Protein Eng. 13, 313-321 (2000).
    • (2000) Protein Eng , vol.13 , pp. 313-321
    • Wray, J.W.1    Baase, W.A.2    Ostheimer, G.J.3    Zhang, X.J.4    Matthews, B.W.5


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