메뉴 건너뛰기




Volumn 46, Issue 27, 2006, Pages 4482-4492

NMR analysis of rhodopsin-transducin interactions

Author keywords

Guanine nucleotide; NMR; Rhodopsin; Signaling; Transducin

Indexed keywords

G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT; RHODOPSIN; TRANSDUCIN;

EID: 33750619233     PISSN: 00426989     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.visres.2006.07.024     Document Type: Article
Times cited : (14)

References (45)
  • 1
    • 0034671530 scopus 로고    scopus 로고
    • Functionally discrete mimics of light-activated rhodopsin identified through expression of soluble cytoplasmic domains
    • Abdulaev N.G., Ngo T., Chen R., Lu Z., and Ridge K.D. Functionally discrete mimics of light-activated rhodopsin identified through expression of soluble cytoplasmic domains. Journal of Biological Chemistry 275 (2000) 39354-39363
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 39354-39363
    • Abdulaev, N.G.1    Ngo, T.2    Chen, R.3    Lu, Z.4    Ridge, K.D.5
  • 2
    • 23144435365 scopus 로고    scopus 로고
    • Bacterial expression and one-step purification of an isotope-labeled heterotrimeric G-protein α-subunit
    • Abdulaev N.G., Zhang C., Dinh A., Ngo T., Bryan P.N., Brabazon D.M., et al. Bacterial expression and one-step purification of an isotope-labeled heterotrimeric G-protein α-subunit. Journal of Biomolecular NMR 32 (2005) 31-40
    • (2005) Journal of Biomolecular NMR , vol.32 , pp. 31-40
    • Abdulaev, N.G.1    Zhang, C.2    Dinh, A.3    Ngo, T.4    Bryan, P.N.5    Brabazon, D.M.6
  • 3
    • 27844496141 scopus 로고    scopus 로고
    • Heterotrimeric G-protein α-subunit adopts a "preactivated" conformation when associated with βγ-subunits
    • Abdulaev N.G., Ngo T., Zhang C., Dinh A., Brabazon D.M., Ridge K.D., et al. Heterotrimeric G-protein α-subunit adopts a "preactivated" conformation when associated with βγ-subunits. Journal of Biological Chemistry 280 (2005) 38071-38080
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 38071-38080
    • Abdulaev, N.G.1    Ngo, T.2    Zhang, C.3    Dinh, A.4    Brabazon, D.M.5    Ridge, K.D.6
  • 4
    • 11244331442 scopus 로고    scopus 로고
    • Phosphatidylethanolamine enhances rhodopsin photoactivation and transducin binding in a solid supported lipid bilayer as determined using plasmon-waveguide resonance spectroscopy
    • Alves I.D., Salgado G.F., Salamon Z., Brown M.F., Tollin G., and Hruby V.J. Phosphatidylethanolamine enhances rhodopsin photoactivation and transducin binding in a solid supported lipid bilayer as determined using plasmon-waveguide resonance spectroscopy. Biophysical Journal 88 (2005) 198-210
    • (2005) Biophysical Journal , vol.88 , pp. 198-210
    • Alves, I.D.1    Salgado, G.F.2    Salamon, Z.3    Brown, M.F.4    Tollin, G.5    Hruby, V.J.6
  • 5
    • 24744444520 scopus 로고    scopus 로고
    • Motion of carboxyl terminus of Gα is restricted upon G protein activation. A solution NMR study using semisynthetic Gα subunits
    • Anderson L.L., Marshall G.R., Crocker E., Smith S.O., and Baranski T.J. Motion of carboxyl terminus of Gα is restricted upon G protein activation. A solution NMR study using semisynthetic Gα subunits. Journal of Biological Chemistry 280 (2005) 31019-31026
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 31019-31026
    • Anderson, L.L.1    Marshall, G.R.2    Crocker, E.3    Smith, S.O.4    Baranski, T.J.5
  • 6
    • 0037457906 scopus 로고    scopus 로고
    • Evidence for structural changes in carboxyl-terminal peptides of transducin α-subunit upon binding a soluble mimic of light-activated rhodopsin
    • Brabazon D.M., Abdulaev N.G., Marino J.P., and Ridge K.D. Evidence for structural changes in carboxyl-terminal peptides of transducin α-subunit upon binding a soluble mimic of light-activated rhodopsin. Biochemistry 42 (2003) 302-311
    • (2003) Biochemistry , vol.42 , pp. 302-311
    • Brabazon, D.M.1    Abdulaev, N.G.2    Marino, J.P.3    Ridge, K.D.4
  • 9
    • 0027495918 scopus 로고
    • Tryptophan W207 in transducin Tα is the fluorescence sensor of the G protein activation switch and is involved in the effector binding
    • Faurobert E., Otto-Bruc A., Chardin P., and Chabre M. Tryptophan W207 in transducin Tα is the fluorescence sensor of the G protein activation switch and is involved in the effector binding. EMBO Journal 12 (1993) 4191-4198
    • (1993) EMBO Journal , vol.12 , pp. 4191-4198
    • Faurobert, E.1    Otto-Bruc, A.2    Chardin, P.3    Chabre, M.4
  • 12
    • 0027787894 scopus 로고
    • The importance of not saturating water in protein NMR. Application to sensitivity enhancement and NOE measurements
    • Grzesiek S., and Bax A. The importance of not saturating water in protein NMR. Application to sensitivity enhancement and NOE measurements. Journal of the American Chemical Society 115 (1993) 12593-12594
    • (1993) Journal of the American Chemical Society , vol.115 , pp. 12593-12594
    • Grzesiek, S.1    Bax, A.2
  • 17
    • 0034093576 scopus 로고    scopus 로고
    • Measurement of dipolar couplings in a transducin peptide fragment weakly bound to oriented photo-activated rhodopsin
    • Koenig B.W., Mitchell D.C., Konig S., Grzesiek S., Litman B.J., and Bax A. Measurement of dipolar couplings in a transducin peptide fragment weakly bound to oriented photo-activated rhodopsin. Journal of Biomolecular NMR 16 (2000) 121-125
    • (2000) Journal of Biomolecular NMR , vol.16 , pp. 121-125
    • Koenig, B.W.1    Mitchell, D.C.2    Konig, S.3    Grzesiek, S.4    Litman, B.J.5    Bax, A.6
  • 18
    • 0036385914 scopus 로고    scopus 로고
    • Structure and orientation of a G protein fragment in the receptor bound state from residual dipolar couplings
    • Koenig B.W., Kontaxis G., Mitchell D.C., Louis J.M., Litman B.J., and Bax A. Structure and orientation of a G protein fragment in the receptor bound state from residual dipolar couplings. Journal of Molecular Biology 322 (2002) 441-461
    • (2002) Journal of Molecular Biology , vol.322 , pp. 441-461
    • Koenig, B.W.1    Kontaxis, G.2    Mitchell, D.C.3    Louis, J.M.4    Litman, B.J.5    Bax, A.6
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0028237708 scopus 로고
    • Structural determinants for activation of the α-subunit of a heterotrimeric G protein
    • Lambright D.G., Noel J.P., Hamm H.E., and Sigler P.B. Structural determinants for activation of the α-subunit of a heterotrimeric G protein. Nature 369 (1994) 621-628
    • (1994) Nature , vol.369 , pp. 621-628
    • Lambright, D.G.1    Noel, J.P.2    Hamm, H.E.3    Sigler, P.B.4
  • 26
    • 0037548053 scopus 로고    scopus 로고
    • Semi-synthesis of proteins by expressed protein ligation
    • Muir T.W. Semi-synthesis of proteins by expressed protein ligation. Annual Review of Biochemistry 72 (2003) 249-289
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 249-289
    • Muir, T.W.1
  • 27
    • 0027132717 scopus 로고
    • The 2.2 Å crystal structure of transducin-α complexed with GTPγS
    • Noel J.P., Hamm H.E., and Sigler P.B. The 2.2 Å crystal structure of transducin-α complexed with GTPγS. Nature 366 (1993) 654-663
    • (1993) Nature , vol.366 , pp. 654-663
    • Noel, J.P.1    Hamm, H.E.2    Sigler, P.B.3
  • 29
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure
    • Okada T., Sugihara M., Bondar A.-N., Elstner M., Entel P., and Buss V. The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure. Journal of Molecular Biology 342 (2004) 571-583
    • (2004) Journal of Molecular Biology , vol.342 , pp. 571-583
    • Okada, T.1    Sugihara, M.2    Bondar, A.-N.3    Elstner, M.4    Entel, P.5    Buss, V.6
  • 32
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson G.L. A simplification of the protein assay method of Lowry et al. which is more generally applicable. Analytical Biochemistry 83 (1977) 346-356
    • (1977) Analytical Biochemistry , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 33
    • 0023708657 scopus 로고
    • The intrinsic fluorescence of the α subunit of transducin. Measurement of receptor-dependent guanine nucleotide exchange
    • Phillips W.J., and Cerione R.A. The intrinsic fluorescence of the α subunit of transducin. Measurement of receptor-dependent guanine nucleotide exchange. Journal of Biological Chemistry 263 (1988) 15498-15505
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 15498-15505
    • Phillips, W.J.1    Cerione, R.A.2
  • 34
    • 0028922277 scopus 로고
    • Structure and function in rhodopsin. Separation and characterization of the correctly folded and misfolded opsins produced on expression of an opsin mutant gene containing only the native intradiscal cysteine codons
    • Ridge K.D., Lu Z., Liu X., and Khorana H.G. Structure and function in rhodopsin. Separation and characterization of the correctly folded and misfolded opsins produced on expression of an opsin mutant gene containing only the native intradiscal cysteine codons. Biochemistry 34 (1995) 3261-3267
    • (1995) Biochemistry , vol.34 , pp. 3261-3267
    • Ridge, K.D.1    Lu, Z.2    Liu, X.3    Khorana, H.G.4
  • 36
    • 33646379375 scopus 로고    scopus 로고
    • Conformational changes associated with receptor-stimulated guanine nucleotide exchange in a heterotrimeric G-protein α-subunit: NMR analysis of GTPγS-bound states
    • Ridge K.D., Abdulaev N.G., Zhang C., Ngo T., Brabazon D.M., and Marino J.P. Conformational changes associated with receptor-stimulated guanine nucleotide exchange in a heterotrimeric G-protein α-subunit: NMR analysis of GTPγS-bound states. Journal of Biological Chemistry 281 (2006) 7635-7648
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 7635-7648
    • Ridge, K.D.1    Abdulaev, N.G.2    Zhang, C.3    Ngo, T.4    Brabazon, D.M.5    Marino, J.P.6
  • 37
    • 8744294716 scopus 로고    scopus 로고
    • Engineering subtilisin into a fluoride-triggered processing protease useful for one-step protein purification
    • Ruan B., Fisher K.E., Alexander P.A., Doroshko V., and Bryan P.N. Engineering subtilisin into a fluoride-triggered processing protease useful for one-step protein purification. Biochemistry 43 (2004) 14539-14546
    • (2004) Biochemistry , vol.43 , pp. 14539-14546
    • Ruan, B.1    Fisher, K.E.2    Alexander, P.A.3    Doroshko, V.4    Bryan, P.N.5
  • 38
    • 0029922635 scopus 로고    scopus 로고
    • Surface plasmon resonance spectroscopy studies of membrane proteins: transducin binding and activation by rhodopsin monitored in thin membrane films
    • Salamon Z., Wang Y., Soulages J.L., Brown M.F., and Tollin G. Surface plasmon resonance spectroscopy studies of membrane proteins: transducin binding and activation by rhodopsin monitored in thin membrane films. Biophysical Journal 71 (1996) 283-294
    • (1996) Biophysical Journal , vol.71 , pp. 283-294
    • Salamon, Z.1    Wang, Y.2    Soulages, J.L.3    Brown, M.F.4    Tollin, G.5
  • 40
    • 0035931919 scopus 로고    scopus 로고
    • Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 Å
    • Slep K.C., Kercher M.A., He W., Cowan C.W., Wensel T.G., and Sigler P.B. Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 Å. Nature 409 (2001) 1071-1077
    • (2001) Nature , vol.409 , pp. 1071-1077
    • Slep, K.C.1    Kercher, M.A.2    He, W.3    Cowan, C.W.4    Wensel, T.G.5    Sigler, P.B.6
  • 43
    • 0035800032 scopus 로고    scopus 로고
    • Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs)
    • Teller D.C., Okada T., Behnke C.A., Palczewski K., and Stenkamp R.E. Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs). Biochemistry 40 (2001) 7761-7772
    • (2001) Biochemistry , vol.40 , pp. 7761-7772
    • Teller, D.C.1    Okada, T.2    Behnke, C.A.3    Palczewski, K.4    Stenkamp, R.E.5
  • 45
    • 0019956634 scopus 로고
    • Light-dependent phosphorylation of rhodopsin: number of phosphorylation sites
    • Wilden U., and Kühn H. Light-dependent phosphorylation of rhodopsin: number of phosphorylation sites. Biochemistry 21 (1982) 3014-3022
    • (1982) Biochemistry , vol.21 , pp. 3014-3022
    • Wilden, U.1    Kühn, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.