메뉴 건너뛰기




Volumn 110, Issue 33, 2013, Pages 13351-13355

Relocating the active-site lysine in rhodopsin and implications for evolution of retinylidene proteins

Author keywords

[No Author keywords available]

Indexed keywords

11 CIS RETINAL; LYSINE; MUTANT PROTEIN; PROTEIN; RETINYLIDENE PROTEIN; RHODOPSIN; TRANSDUCIN; UNCLASSIFIED DRUG;

EID: 84882366844     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1306826110     Document Type: Article
Times cited : (25)

References (42)
  • 2
    • 84873685831 scopus 로고    scopus 로고
    • Molecular signatures of G-protein-coupled receptors
    • Venkatakrishnan AJ, et al. (2013) Molecular signatures of G-protein-coupled receptors. Nature 494(7436):185-194.
    • (2013) Nature , vol.494 , Issue.7436 , pp. 185-194
    • Venkatakrishnan, A.J.1
  • 3
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C (1995) SCOP: A structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 247(4):536-540.
    • (1995) J Mol Biol , vol.247 , Issue.4 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 4
    • 84855845956 scopus 로고    scopus 로고
    • Chemistry and biology of vision
    • Palczewski K (2012) Chemistry and biology of vision. J Biol Chem 287(3):1612-1619.
    • (2012) J Biol Chem , vol.287 , Issue.3 , pp. 1612-1619
    • Palczewski, K.1
  • 5
    • 77952906089 scopus 로고    scopus 로고
    • Structure and activation of the visual pigment rhodopsin
    • Smith SO (2010) Structure and activation of the visual pigment rhodopsin. Annu Rev Biophys 39:309-328.
    • (2010) Annu Rev Biophys , vol.39 , pp. 309-328
    • Smith, S.O.1
  • 6
    • 84876578144 scopus 로고    scopus 로고
    • New functional families (FunFams) in CATH to improve the mapping of conserved functional sites to 3D structures
    • Sillitoe I, et al. (2013) New functional families (FunFams) in CATH to improve the mapping of conserved functional sites to 3D structures. Nucleic Acids Res 41(Database issue):D490-D498.
    • (2013) Nucleic Acids Res 41(Database Issue)
    • Sillitoe, I.1
  • 7
    • 44249096288 scopus 로고    scopus 로고
    • Type II opsins Evolutionary origin by internal domain duplication?
    • Larusso ND, Ruttenberg BE, Singh AK, Oakley TH (2008) Type II opsins: Evolutionary origin by internal domain duplication? J Mol Evol 66(5):417-423.
    • (2008) J Mol Evol , vol.66 , Issue.5 , pp. 417-423
    • Larusso, N.D.1    Ruttenberg, B.E.2    Singh, A.K.3    Oakley, T.H.4
  • 8
    • 0028262380 scopus 로고
    • Two hypotheses - One answer 0Sequence comparison does not support an evolutionary link between halobacterial retinal proteins including bacteriorhodopsin and eukaryotic G-protein-coupled receptors
    • Soppa J (1994) Two hypotheses - one answer. Sequence comparison does not support an evolutionary link between halobacterial retinal proteins including bacteriorhodopsin and eukaryotic G-protein-coupled receptors. FEBS Lett 342(1):7-11.
    • (1994) FEBS Lett , vol.342 , Issue.1 , pp. 7-11
    • Soppa, J.1
  • 9
    • 70349928636 scopus 로고    scopus 로고
    • The predictability of evolution: Glimpses into a post- Darwinian world
    • Conway Morris S (2009) The predictability of evolution: Glimpses into a post- Darwinian world. Naturwissenschaften 96(11):1313-1337.
    • (2009) Naturwissenschaften , vol.96 , Issue.11 , pp. 1313-1337
    • Conway Morris, S.1
  • 10
    • 84882379316 scopus 로고    scopus 로고
    • Oxford Univ Press Oxford 2nd Ed, pp xiii, 271 of plates
    • Land MF, Nilsson D-E (2012) Animal Eyes (Oxford Univ Press, Oxford) 2nd Ed, pp xiii, 271 pp, 274 pp of plates.
    • (2012) Animal Eyes , pp. 274
    • Land, M.F.1    Nilsson, D.-E.2
  • 11
    • 49549116213 scopus 로고    scopus 로고
    • On the origins of arrestin and rhodopsin
    • Alvarez CE (2008) On the origins of arrestin and rhodopsin. BMC Evol Biol 8:222.
    • (2008) BMC Evol Biol , vol.8 , pp. 222
    • Alvarez, C.E.1
  • 12
    • 77955382760 scopus 로고    scopus 로고
    • The evolution of phototransduction from an ancestral cyclic nucleotide gated pathway
    • Plachetzki DC, Fong CR, Oakley TH (2010) The evolution of phototransduction from an ancestral cyclic nucleotide gated pathway. Proc Biol Sci 277(1690):1963-1969.
    • (2010) Proc Biol Sci , vol.277 , pp. 1963-1969
    • Plachetzki, D.C.1    Fong, C.R.2    Oakley, T.H.3
  • 13
    • 0025757195 scopus 로고
    • Transducin activation by rhodopsin without a covalent bond to the 11-cis-retinal chromophore
    • Zhukovsky EA, Robinson PR, Oprian DD (1991) Transducin activation by rhodopsin without a covalent bond to the 11-cis-retinal chromophore. Science 251(4993): 558-560.
    • (1991) Science , vol.251 , Issue.4993 , pp. 558-560
    • Zhukovsky, E.A.1    Robinson, P.R.2    Oprian, D.D.3
  • 15
    • 0025162902 scopus 로고
    • Determinants of visual pigment absorbance: Identification of the retinylidene Schiff's base counterion in bovine rhodopsin
    • Nathans J (1990) Determinants of visual pigment absorbance: Identification of the retinylidene Schiff's base counterion in bovine rhodopsin. Biochemistry 29(41): 9746-9752.
    • (1990) Biochemistry , vol.29 , Issue.41 , pp. 9746-9752
    • Nathans, J.1
  • 16
    • 0343177634 scopus 로고
    • Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin
    • Sakmar TP, Franke RR, Khorana HG (1989) Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin. Proc Natl Acad Sci USA 86(21): 8309-8313.
    • (1989) Proc Natl Acad Sci USA , vol.86 , Issue.21 , pp. 8309-8313
    • Sakmar, T.P.1    Franke, R.R.2    Khorana, H.G.3
  • 17
    • 0024362631 scopus 로고
    • Effect of carboxylic acid side chains on the absorption maximum of visual pigments
    • Zhukovsky EA, Oprian DD (1989) Effect of carboxylic acid side chains on the absorption maximum of visual pigments. Science 246(4932):928-930.
    • (1989) Science , vol.246 , Issue.4932 , pp. 928-930
    • Zhukovsky, E.A.1    Oprian, D.D.2
  • 18
    • 34249040518 scopus 로고    scopus 로고
    • Protein design: Reengineering cellular retinoic acid binding protein II into a rhodopsin protein mimic
    • Vasileiou C, et al. (2007) Protein design: Reengineering cellular retinoic acid binding protein II into a rhodopsin protein mimic. J Am Chem Soc 129(19):6140-6148.
    • (2007) J Am Chem Soc , vol.129 , Issue.19 , pp. 6140-6148
    • Vasileiou, C.1
  • 19
    • 84870696480 scopus 로고    scopus 로고
    • Tuning the electronic absorption of protein-embedded alltrans- retinal
    • Wang W, et al. (2012) Tuning the electronic absorption of protein-embedded alltrans- retinal. Science 338(6112):1340-1343.
    • (2012) Science , vol.338 , Issue.6112 , pp. 1340-1343
    • Wang, W.1
  • 20
    • 59649112109 scopus 로고    scopus 로고
    • Helix movement is coupled to displacement of the second extracellular loop in rhodopsin activation
    • Ahuja S, et al. (2009) Helix movement is coupled to displacement of the second extracellular loop in rhodopsin activation. Nat Struct Mol Biol 16(2):168-175.
    • (2009) Nat Struct Mol Biol , vol.16 , Issue.2 , pp. 168-175
    • Ahuja, S.1
  • 22
    • 84888203347 scopus 로고    scopus 로고
    • Biochemistry 37(22):8253-8261.
    • Biochemistry , vol.37 , Issue.22 , pp. 8253-8261
  • 23
    • 35649004285 scopus 로고    scopus 로고
    • Engineering a "steric doorstop" in rhodopsin: Converting an inverse agonist to an agonist
    • McKee TD, Lewis MR, Kono M (2007) Engineering a "steric doorstop" in rhodopsin: Converting an inverse agonist to an agonist. Biochemistry 46(43):12248-12252.
    • (2007) Biochemistry , vol.46 , Issue.43 , pp. 12248-12252
    • McKee, T.D.1    Lewis, M.R.2    Kono, M.3
  • 24
    • 0033901466 scopus 로고    scopus 로고
    • Effect of 11-cis 13-demethylretinal on phototransduction in bleach-adapted rod and cone photoreceptors
    • Corson DW, Kefalov VJ, Cornwall MC, Crouch RK (2000) Effect of 11-cis 13-demethylretinal on phototransduction in bleach-adapted rod and cone photoreceptors. J Gen Physiol 116(2):283-297.
    • (2000) J Gen Physiol , vol.116 , Issue.2 , pp. 283-297
    • Corson, D.W.1    Kefalov, V.J.2    Cornwall, M.C.3    Crouch, R.K.4
  • 25
    • 0035046325 scopus 로고    scopus 로고
    • Role of noncovalent binding of 11-cisretinal to opsin in dark adaptation of rod and cone photoreceptors
    • Kefalov VJ, Crouch RK, Cornwall MC (2001) Role of noncovalent binding of 11-cisretinal to opsin in dark adaptation of rod and cone photoreceptors. Neuron 29(3): 749-755.
    • (2001) Neuron , vol.29 , Issue.3 , pp. 749-755
    • Kefalov, V.J.1    Crouch, R.K.2    Cornwall, M.C.3
  • 26
    • 20444371505 scopus 로고    scopus 로고
    • Breaking the covalent bond - A pigment property that contributes to desensitization in cones
    • Kefalov VJ, et al. (2005) Breaking the covalent bond - a pigment property that contributes to desensitization in cones. Neuron 46(6):879-890.
    • (2005) Neuron , vol.46 , Issue.6 , pp. 879-890
    • Kefalov, V.J.1
  • 27
    • 0026475571 scopus 로고
    • Changing the location of the Schiff base counterion in rhodopsin
    • Zhukovsky EA, Robinson PR, Oprian DD (1992) Changing the location of the Schiff base counterion in rhodopsin. Biochemistry 31(42):10400-10405.
    • (1992) Biochemistry , vol.31 , Issue.42 , pp. 10400-10405
    • Zhukovsky, E.A.1    Robinson, P.R.2    Oprian, D.D.3
  • 28
    • 0028128646 scopus 로고
    • Characterization of rhodopsin-transducin interaction: A mutant rhodopsin photoproduct with a protonated Schiff base activates transducin
    • Zvyaga TA, Fahmy K, Sakmar TP (1994) Characterization of rhodopsin-transducin interaction: A mutant rhodopsin photoproduct with a protonated Schiff base activates transducin. Biochemistry 33(32):9753-9761.
    • (1994) Biochemistry , vol.33 , Issue.32 , pp. 9753-9761
    • Zvyaga, T.A.1    Fahmy, K.2    Sakmar, T.P.3
  • 29
    • 0028102745 scopus 로고
    • A mutant rhodopsin photoproduct with a protonated Schiff base displays an active-state conformation: A Fourier-transform infrared spectroscopy study
    • Fahmy K, Siebert F, Sakmar TP (1994) A mutant rhodopsin photoproduct with a protonated Schiff base displays an active-state conformation: A Fourier-transform infrared spectroscopy study. Biochemistry 33(46):13700-13705.
    • (1994) Biochemistry , vol.33 , Issue.46 , pp. 13700-13705
    • Fahmy, K.1    Siebert, F.2    Sakmar, T.P.3
  • 30
    • 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 KD, Lu Z, Liu X, Khorana HG (1995) 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(10):3261-3267.
    • (1995) Biochemistry , vol.34 , Issue.10 , pp. 3261-3267
    • Ridge, K.D.1    Lu, Z.2    Liu, X.3    Khorana, H.G.4
  • 31
    • 0037465339 scopus 로고    scopus 로고
    • An opsin mutant with increased thermal stability
    • Xie G, Gross AK, Oprian DD (2003) An opsin mutant with increased thermal stability. Biochemistry 42(7):1995-2001.
    • (2003) Biochemistry , vol.42 , Issue.7 , pp. 1995-2001
    • Xie, G.1    Gross, A.K.2    Oprian, D.D.3
  • 32
    • 81855226606 scopus 로고    scopus 로고
    • Preparation of an activated rhodopsin/transducin complex using a constitutively active mutant of rhodopsin
    • Xie G, et al. (2011) Preparation of an activated rhodopsin/transducin complex using a constitutively active mutant of rhodopsin. Biochemistry 50(47):10399-10407.
    • (2011) Biochemistry , vol.50 , Issue.47 , pp. 10399-10407
    • Xie, G.1
  • 33
    • 0037465424 scopus 로고    scopus 로고
    • Slow binding of retinal to rhodopsin mutants G90D and T94D
    • Gross AK, Xie G, Oprian DD (2003) Slow binding of retinal to rhodopsin mutants G90D and T94D. Biochemistry 42(7):2002-2008.
    • (2003) Biochemistry , vol.42 , Issue.7 , pp. 2002-2008
    • Gross, A.K.1    Xie, G.2    Oprian, D.D.3
  • 34
    • 34548529916 scopus 로고    scopus 로고
    • Crystal structure of a thermally stable rhodopsin mutant
    • Standfuss J, et al. (2007) Crystal structure of a thermally stable rhodopsin mutant. J Mol Biol 372(5):1179-1188.
    • (2007) J Mol Biol , vol.372 , Issue.5 , pp. 1179-1188
    • Standfuss, J.1
  • 35
    • 84855990615 scopus 로고    scopus 로고
    • Stabilized G protein binding site in the structure of constitutively active metarhodopsin-II
    • Deupi X, et al. (2012) Stabilized G protein binding site in the structure of constitutively active metarhodopsin-II. Proc Natl Acad Sci USA 109(1):119-124.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.1 , pp. 119-124
    • Deupi, X.1
  • 36
    • 79953242234 scopus 로고    scopus 로고
    • The structural basis of agonist-induced activation in constitutively active rhodopsin
    • Standfuss J, et al. (2011) The structural basis of agonist-induced activation in constitutively active rhodopsin. Nature 471(7340):656-660.
    • (2011) Nature , vol.471 , Issue.7340 , pp. 656-660
    • Standfuss, J.1
  • 37
    • 79953234218 scopus 로고    scopus 로고
    • Crystal structure of metarhodopsin II
    • Choe HW, et al. (2011) Crystal structure of metarhodopsin II. Nature 471(7340): 651-655.
    • (2011) Nature , vol.471 , Issue.7340 , pp. 651-655
    • Choe, H.W.1
  • 38
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • Palczewski K, et al. (2000) Crystal structure of rhodopsin: A G protein-coupled receptor. Science 289(5480):739-745.
    • (2000) Science , vol.289 , Issue.5480 , pp. 739-745
    • Palczewski, K.1
  • 39
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • Park JH, Scheerer P, Hofmann KP, Choe HW, Ernst OP (2008) Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 454(7201):183-187.
    • (2008) Nature , vol.454 , Issue.7201 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.W.4    Ernst, O.P.5
  • 40
    • 52949102889 scopus 로고    scopus 로고
    • Crystal structure of opsin in its G-protein-interacting conformation
    • Scheerer P, et al. (2008) Crystal structure of opsin in its G-protein-interacting conformation. Nature 455(7212):497-502.
    • (2008) Nature , vol.455 , Issue.7212 , pp. 497-502
    • Scheerer, P.1
  • 41
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous Nglycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • Reeves PJ, Callewaert N, Contreras R, Khorana HG (2002) Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous Nglycosylation by a tetracycline-inducible N- acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc Natl Acad Sci USA 99(21):13419-13424.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.21 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 42
    • 0033533398 scopus 로고    scopus 로고
    • Spectral tuning in the human blue cone pigment
    • Fasick JI, Lee N, Oprian DD (1999) Spectral tuning in the human blue cone pigment. Biochemistry 38(36):11593-11596.
    • (1999) Biochemistry , vol.38 , Issue.36 , pp. 11593-11596
    • Fasick, J.I.1    Lee, N.2    Oprian, D.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.