메뉴 건너뛰기




Volumn 87, Issue 3, 1996, Pages 577-588

Crystal structure at 2.4 Å resolution of the complex of transducin βγ and its regulator, phosducin

Author keywords

[No Author keywords available]

Indexed keywords

PHOSDUCIN; PROTEIN SUBUNIT; REGULATOR PROTEIN; SERINE; THIOREDOXIN; TRANSDUCIN;

EID: 0030297912     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81376-8     Document Type: Article
Times cited : (273)

References (49)
  • 3
    • 0030576518 scopus 로고    scopus 로고
    • GAIP and RGS4 are GTPase activating proteins (GAPs) for the Gi subfamily of G protein α subunits
    • Berman, D.M., Wilkie, T.M., and Gilman, A.G. (1996). GAIP and RGS4 are GTPase activating proteins (GAPs) for the Gi subfamily of G protein α subunits. Cell 86, 445-452.
    • (1996) Cell , vol.86 , pp. 445-452
    • Berman, D.M.1    Wilkie, T.M.2    Gilman, A.G.3
  • 4
    • 0028068336 scopus 로고
    • Purification of Tβγ subunit of transducin
    • Bigay, J., and Chabre, M. (1994). Purification of Tβγ subunit of transducin. Meth. Enzymol. 237, 449-451.
    • (1994) Meth. Enzymol. , vol.237 , pp. 449-451
    • Bigay, J.1    Chabre, M.2
  • 6
    • 0001037624 scopus 로고
    • Algorithm for ribbon models of proteins
    • Carson, M., and Bugg, C.E. (1986). Algorithm for ribbon models of proteins. J. Mol. Graphics 4, 121-122.
    • (1986) J. Mol. Graphics , vol.4 , pp. 121-122
    • Carson, M.1    Bugg, C.E.2
  • 7
    • 0025989987 scopus 로고
    • Rat pineal gland phosducin: cDNA isolation, nucleotide sequence, and chromosomal assignment in the mouse
    • Craft, C.M., Lolley, R.N., Seldin, M.F., and Lee, R.H. (1991). Rat pineal gland phosducin: cDNA isolation, nucleotide sequence, and chromosomal assignment in the mouse. Genomics 10, 400-409.
    • (1991) Genomics , vol.10 , pp. 400-409
    • Craft, C.M.1    Lolley, R.N.2    Seldin, M.F.3    Lee, R.H.4
  • 8
    • 0027495684 scopus 로고
    • New roles for G-protein βγ-dimers in transmembrane signaling
    • Clapham, D.E., and Neer, E.J. (1993). New roles for G-protein βγ-dimers in transmembrane signaling. Nature 365, 403-406.
    • (1993) Nature , vol.365 , pp. 403-406
    • Clapham, D.E.1    Neer, E.J.2
  • 10
    • 84913074520 scopus 로고
    • Anomalous dispersion calculation near to and on the long-wavelength side of an absorption edge
    • Cromer, D.T., and Liberman, D.A. (1981). Anomalous dispersion calculation near to and on the long-wavelength side of an absorption edge. Acta Crystallogr. A37, 267-268.
    • (1981) Acta Crystallogr. , vol.A37 , pp. 267-268
    • Cromer, D.T.1    Liberman, D.A.2
  • 11
    • 0029814150 scopus 로고    scopus 로고
    • Phosducin is a ubiquitous G-protein regulator
    • Danner, S., and Lohse, M.J. (1996). Phosducin is a ubiquitous G-protein regulator. Proc. Natl. Acad. Sci. USA 93, 10145-10150.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10145-10150
    • Danner, S.1    Lohse, M.J.2
  • 13
    • 0027000604 scopus 로고
    • Rhodopsin and photo-transduction
    • Hargrave, P.A., and McDowell, J.H. (1992). Rhodopsin and photo-transduction. Int. Rev. Cytol. 137B, 49-97.
    • (1992) Int. Rev. Cytol. , vol.137 B , pp. 49-97
    • Hargrave, P.A.1    McDowell, J.H.2
  • 14
    • 0028171681 scopus 로고
    • Determination of the Gβγ-binding domain of phosducin. A regulatable modulator of Gβγ signaling
    • Hawes, B.E., Touhara, K., Kurose, H., Lefkowitz, R.J., and Inglese, J. (1994). Determination of the Gβγ-binding domain of phosducin. A regulatable modulator of Gβγ signaling. J. Biol. Chem. 269, 29825-29830.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29825-29830
    • Hawes, B.E.1    Touhara, K.2    Kurose, H.3    Lefkowitz, R.J.4    Inglese, J.5
  • 15
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction: Solvation properties of penicillopepsin and neuraminidase crystal structures
    • Jiang, J.-S., and Brünger, A.T. (1994). Protein hydration observed by X-ray diffraction: solvation properties of penicillopepsin and neuraminidase crystal structures. J. Mol. Biol. 243, 100-115.
    • (1994) J. Mol. Biol. , vol.243 , pp. 100-115
    • Jiang, J.-S.1    Brünger, A.T.2
  • 16
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of error in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W., and Kheldjaard, M. (1991). Improved methods for building protein models in electron density maps and the location of error in these models. Acta Crystallgr. A47, 110-119.
    • (1991) Acta Crystallgr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kheldjaard, M.4
  • 17
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 18
    • 0025319619 scopus 로고
    • Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution
    • Katti, S.K., LeMaster D.M., and Eklund, H. (1990). Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution. J. Mol. Biol. 212, 167-184.
    • (1990) J. Mol. Biol. , vol.212 , pp. 167-184
    • Katti, S.K.1    LeMaster, D.M.2    Eklund, H.3
  • 19
    • 0028237708 scopus 로고
    • Structural determinants for the activation of the α-subunit of a heterotrimeric G protein
    • Lambright, D.G., Noel, J.P., Hamm, H.E., and Sigler, P.B. (1994). Structural determinants for the activation of the α-subunit of a heterotrimeric G protein. Nature 369, 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
  • 21
    • 0023904701 scopus 로고
    • The photoreceptor-specific 33 kDa phosphoprotein of mammalian retina: Generation of monospecific antibodies and localization by immunocytochemistry
    • Lee, R.H., Whelan, J.P., Lolley, R.N., and McGinnis, J.F. (1988). The photoreceptor-specific 33 kDa phosphoprotein of mammalian retina: generation of monospecific antibodies and localization by immunocytochemistry. Exp. Eye Res. 46, 829-840.
    • (1988) Exp. Eye Res. , vol.46 , pp. 829-840
    • Lee, R.H.1    Whelan, J.P.2    Lolley, R.N.3    McGinnis, J.F.4
  • 22
    • 0025181060 scopus 로고
    • Protein kinase A phosphorylates retinal phosducin on serine 73 in situ
    • Lee, R.H., Brown, B.M., and Lolley, R.N. (1990a). Protein kinase A phosphorylates retinal phosducin on serine 73 in situ. J. Biol. Chem. 265, 15860-15866.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15860-15866
    • Lee, R.H.1    Brown, B.M.2    Lolley, R.N.3
  • 23
    • 0025161420 scopus 로고
    • Retinal accumulation of the phosducin/Tβγ and transducin complexes in developing normal mice and in mice and dogs with inherited retinal degeneration
    • Lee, R.H., Lieberman, B.S., and Lolley, R.N. (1990b). Retinal accumulation of the phosducin/Tβγ and transducin complexes in developing normal mice and in mice and dogs with inherited retinal degeneration. Exp. Eye Res. 51, 325-333.
    • (1990) Exp. Eye Res. , vol.51 , pp. 325-333
    • Lee, R.H.1    Lieberman, B.S.2    Lolley, R.N.3
  • 24
    • 0029939448 scopus 로고    scopus 로고
    • PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surface
    • Lemmon, M.A., Ferguson, K.M., and Schlessinger, J. (1996). PH domains: diverse sequences with a common fold recruit signaling molecules to the cell surface. Cell 85, 621-624.
    • (1996) Cell , vol.85 , pp. 621-624
    • Lemmon, M.A.1    Ferguson, K.M.2    Schlessinger, J.3
  • 25
    • 0025260486 scopus 로고
    • Cyclic GMP and photoreceptor function
    • Lolley, R.N., and Lee, R.H. (1990). Cyclic GMP and photoreceptor function. FASEB J. 4, 3001-3008.
    • (1990) FASEB J. , vol.4 , pp. 3001-3008
    • Lolley, R.N.1    Lee, R.H.2
  • 27
    • 0029165589 scopus 로고
    • Thioredoxin - A fold for all reasons
    • Martin, J.L. (1995). Thioredoxin - a fold for all reasons. Structure 3, 245-250.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 28
    • 0027449386 scopus 로고
    • Phosducin-like protein: An ethanol-responsive potential modulator of guanine nucleotide-binding protein function
    • Miles, M.F., Barhite, S., Sganga, M., and Elliott, M. (1993). Phosducin-like protein: an ethanol-responsive potential modulator of guanine nucleotide-binding protein function. Proc. Natl. Acad. Sci. USA 90, 10831-10835.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10831-10835
    • Miles, M.F.1    Barhite, S.2    Sganga, M.3    Elliott, M.4
  • 29
    • 0027936706 scopus 로고
    • Aluminum fluoride activation of bovine transducin induces two distinct conformational changes in the α subunit
    • Mittal, R., Cerione, R.A., and Erickson, J.W. (1994). Aluminum fluoride activation of bovine transducin induces two distinct conformational changes in the α subunit. Biochemistry 33, 10178-10184.
    • (1994) Biochemistry , vol.33 , pp. 10178-10184
    • Mittal, R.1    Cerione, R.A.2    Erickson, J.W.3
  • 30
    • 0038409097 scopus 로고    scopus 로고
    • Interactions of phosducin with defined G protein βγ-subunits
    • Müller, S., Straub, A., Schöder, S., Bauer, P.H., and Lohse, M.J. (1996). Interactions of phosducin with defined G protein βγ-subunits. J. Biol. Chem. 271, 11781-11786.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11781-11786
    • Müller, S.1    Straub, A.2    Schöder, S.3    Bauer, P.H.4    Lohse, M.J.5
  • 31
    • 0028076764 scopus 로고
    • The ancient regulatory-protein family of WD-repeat proteins
    • Neer, E.J., Schmidt, C.J., Mambudripad, R., and Smith, T.F. (1994). The ancient regulatory-protein family of WD-repeat proteins. Nature 371, 297-300.
    • (1994) Nature , vol.371 , pp. 297-300
    • Neer, E.J.1    Schmidt, C.J.2    Mambudripad, R.3    Smith, T.F.4
  • 33
    • 84986486656 scopus 로고
    • A rapid finite difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation
    • Nicholls, A., and Honig, B.J. (1991). A rapid finite difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation. J. Comp. Chem. 12, 435-445.
    • (1991) J. Comp. Chem. , vol.12 , pp. 435-445
    • Nicholls, A.1    Honig, B.J.2
  • 34
    • 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. (1993). The 2.2 Å crystal structure of transducin-α complexed with GTPγS. Nature 366, 654-663.
    • (1993) Nature , vol.366 , pp. 654-663
    • Noel, J.P.1    Hamm, H.E.2    Sigler, P.B.3
  • 35
    • 0028789263 scopus 로고
    • Phosducin and PP33 are in vivo targets of PKA and type 1 or 2A phosphatases, regulators of cell elongation in teleost rod inner-outer segments
    • Pagh-Roehl, K., Lin, D., Su, L, and Burnside, B. (1995). Phosducin and PP33 are in vivo targets of PKA and type 1 or 2A phosphatases, regulators of cell elongation in teleost rod inner-outer segments. J. Neurosci. 15, 6475-6488.
    • (1995) J. Neurosci. , vol.15 , pp. 6475-6488
    • Pagh-Roehl, K.1    Lin, D.2    Su, L.3    Burnside, B.4
  • 37
    • 0029002493 scopus 로고
    • A direct interaction between G-protein βγ subunits and the Raf-1 protein kinase
    • Pumiglia, K.M., LeVine, H., Haske, T., Habib, T., Jove, R., and Decker, S.J. (1995). A direct interaction between G-protein βγ subunits and the Raf-1 protein kinase. J. Biol. Chem. 270, 14251-14254.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14251-14254
    • Pumiglia, K.M.1    LeVine, H.2    Haske, T.3    Habib, T.4    Jove, R.5    Decker, S.J.6
  • 38
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. (1986). Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallgr. A42, 140-149.
    • (1986) Acta Crystallgr. , vol.A42 , pp. 140-149
    • Read, R.J.1
  • 39
    • 0025236741 scopus 로고
    • Pineal transduction. Adrenergiccyclic AMP-dependent phosphorylation of cytoplasmic 33-kDa protein (MEKA) which binds βγ-complex of transducin
    • Reig, J.A., Yu, L., and Klein, D.C. (1990). Pineal Transduction. Adrenergiccyclic AMP-dependent phosphorylation of cytoplasmic 33-kDa protein (MEKA) which binds βγ-complex of transducin. J. Biol. Chem. 265, 5816-5824.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5816-5824
    • Reig, J.A.1    Yu, L.2    Klein, D.C.3
  • 40
    • 0029935648 scopus 로고    scopus 로고
    • Inhibition of G-protein βγ-subunit functions by phosducin-like protein
    • Schröder, S., and Lohse, M.J. (1996). Inhibition of G-protein βγ-subunit functions by phosducin-like protein. Proc. Natl. Acad. Sci. USA 93, 2100-2104.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2100-2104
    • Schröder, S.1    Lohse, M.J.2
  • 41
    • 84943920736 scopus 로고
    • Phase annealing in SHELX-90: Direct methods for larger structures
    • Sheldrick, G.M. (1990). Phase annealing in SHELX-90: direct methods for larger structures. Acta Crystallgr. A46, 467-473.
    • (1990) Acta Crystallgr. , vol.A46 , pp. 467-473
    • Sheldrick, G.M.1
  • 43
    • 0030034646 scopus 로고    scopus 로고
    • Crystal structure of a G protein βγ dimer at 2.1 Å resolution
    • Sondek, J., Bohm, A., Lambright, D.G., Hamm, H.E., and Sigler, P.B. (1996). Crystal structure of a G protein βγ dimer at 2.1 Å resolution. Nature 379, 369-374.
    • (1996) Nature , vol.379 , pp. 369-374
    • Sondek, J.1    Bohm, A.2    Lambright, D.G.3    Hamm, H.E.4    Sigler, P.B.5
  • 46
    • 0029739635 scopus 로고    scopus 로고
    • Regulation of the kinetics of phosducin phosphorylation in retinal rods
    • Wilkins, J.F., Bitensky, M.W., and Willardson, B.M. (1996). Regulation of the kinetics of phosducin phosphorylation in retinal rods. J. Biol. Chem. 277, 19232-19237.
    • (1996) J. Biol. Chem. , vol.277 , pp. 19232-19237
    • Wilkins, J.F.1    Bitensky, M.W.2    Willardson, B.M.3
  • 48
    • 0028968341 scopus 로고
    • The N terminus of phosducin is involved in binding of βγ subunits of G protein
    • Xu, J., Wu, D., Slepak, V.Z., and Simon, M.I. (1995). The N terminus of phosducin is involved in binding of βγ subunits of G protein. Proc. Natl. Acad. Sci. USA 92, 2086-2090.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2086-2090
    • Xu, J.1    Wu, D.2    Slepak, V.Z.3    Simon, M.I.4
  • 49
    • 0027971161 scopus 로고
    • The phosphorylation state of phosducin determines its ability to block transducin subunit interactions and inhibit transducin binding to activated rhodopsin
    • Yoshida, T., Willardson, B.M., Wilkins, J.F., Jensen, G.J., Thornton, B.D., and Bitensky, M.W. (1994). The phosphorylation state of phosducin determines its ability to block transducin subunit interactions and inhibit transducin binding to activated rhodopsin. J. Biol. Chem. 269, 24050-24057.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24050-24057
    • Yoshida, T.1    Willardson, B.M.2    Wilkins, J.F.3    Jensen, G.J.4    Thornton, B.D.5    Bitensky, M.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.