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Volumn 73, Issue 7, 2008, Pages 708-719

Homology modelling of human DHCR24 (seladin-1) and analysis of its binding properties through molecular docking and dynamics simulations

Author keywords

Cholesterol biosynthesis; DHCR24; Enzymatic product egress; Homology modelling; MD simulation; Seladin 1

Indexed keywords

3 BETA HYDROXYSTEROL REDUCTASE; CHOLESTEROL; CYTOKININ; DESMOSTEROL; ENZYME; OXIDOREDUCTASE; SELADIN 1;

EID: 43649109013     PISSN: 0039128X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.steroids.2008.02.007     Document Type: Article
Times cited : (18)

References (42)
  • 1
    • 0034307463 scopus 로고    scopus 로고
    • The human DIMINUTO/DWARF1 homolog seladin-1 confers resistance to Alzheimer's disease-associated neurodegeneration and oxidative stress
    • Greeve I., Hermans-Borgmeyer I., Brellinger C., Kasper D., Gomez-Isla T., Behl C., et al. The human DIMINUTO/DWARF1 homolog seladin-1 confers resistance to Alzheimer's disease-associated neurodegeneration and oxidative stress. J Neurosci 20 (2000) 7345-7352
    • (2000) J Neurosci , vol.20 , pp. 7345-7352
    • Greeve, I.1    Hermans-Borgmeyer, I.2    Brellinger, C.3    Kasper, D.4    Gomez-Isla, T.5    Behl, C.6
  • 2
    • 0034741599 scopus 로고    scopus 로고
    • Mutations in the 3beta-hydroxysterol Delta24-reductase gene cause desmosterolosis, an autosomal recessive disorder of cholesterol biosynthesis
    • Waterham H.R., Koster J., Romeijn G.J., Hennekam R.C., Vreken P., Andersson H.C., et al. Mutations in the 3beta-hydroxysterol Delta24-reductase gene cause desmosterolosis, an autosomal recessive disorder of cholesterol biosynthesis. Am J Hum Genet 69 (2001) 685-694
    • (2001) Am J Hum Genet , vol.69 , pp. 685-694
    • Waterham, H.R.1    Koster, J.2    Romeijn, G.J.3    Hennekam, R.C.4    Vreken, P.5    Andersson, H.C.6
  • 3
    • 0030858044 scopus 로고    scopus 로고
    • Cholesterol biosynthesis from lanosterol: development of a novel assay method and characterization of rat liver microsomal lanosterol delta 24-reductase
    • Bae S.H., and Paik Y.K. Cholesterol biosynthesis from lanosterol: development of a novel assay method and characterization of rat liver microsomal lanosterol delta 24-reductase. Biochem J 326 (1997) 609-616
    • (1997) Biochem J , vol.326 , pp. 609-616
    • Bae, S.H.1    Paik, Y.K.2
  • 4
    • 0029026444 scopus 로고
    • A putative FAD-binding domain in a distinct group of oxidases including a protein involved in plant development
    • Mushegian A.R., and Koonin E.V. A putative FAD-binding domain in a distinct group of oxidases including a protein involved in plant development. Protein Sci 4 (1995) 1243-1244
    • (1995) Protein Sci , vol.4 , pp. 1243-1244
    • Mushegian, A.R.1    Koonin, E.V.2
  • 5
    • 0032192096 scopus 로고    scopus 로고
    • The Arabidopsis DIMINUTO/DWARF1 gene encodes a protein involved in steroid synthesis
    • Klahre U., Noguchi T., Fujioka S., Takatsuto S., Yokota T., Nomura T., et al. The Arabidopsis DIMINUTO/DWARF1 gene encodes a protein involved in steroid synthesis. Plant Cell 10 (1998) 1677-1690
    • (1998) Plant Cell , vol.10 , pp. 1677-1690
    • Klahre, U.1    Noguchi, T.2    Fujioka, S.3    Takatsuto, S.4    Yokota, T.5    Nomura, T.6
  • 6
    • 0037114662 scopus 로고    scopus 로고
    • Desmosterolosis presenting with multiple congenital anomalies and profound developmental delay
    • Andersson H.C., Kratz L., and Kelley R. Desmosterolosis presenting with multiple congenital anomalies and profound developmental delay. Am J Med Genet 113 (2002) 315-319
    • (2002) Am J Med Genet , vol.113 , pp. 315-319
    • Andersson, H.C.1    Kratz, L.2    Kelley, R.3
  • 8
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi J., Blundell T.L., and Mizuguchi K. FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J Mol Biol 310 (2001) 243-257
    • (2001) J Mol Biol , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 9
    • 0031574072 scopus 로고    scopus 로고
    • The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 24 (1997) 4876-4882
    • (1997) Nucleic Acids Res , vol.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 10
    • 0036284090 scopus 로고    scopus 로고
    • VEGA: a versatile program to convert, handle and visualize molecular structure on windows-based PCs
    • Pedretti A., Villa L., and Vistoli G. VEGA: a versatile program to convert, handle and visualize molecular structure on windows-based PCs. J Mol Graph 21 (2002) 47-49
    • (2002) J Mol Graph , vol.21 , pp. 47-49
    • Pedretti, A.1    Villa, L.2    Vistoli, G.3
  • 11
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 26 (1993) 283-291
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 12
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie J.U., Luthy R., and Eisenberg D. A method to identify protein sequences that fold into a known three-dimensional structure. Science 253 (1991) 164-170
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.3
  • 13
    • 0000207681 scopus 로고
    • TMbase-a database of membrane spanning proteins segments
    • Hofmann K., and Stoffel W. TMbase-a database of membrane spanning proteins segments. Biol Chem Hoppe-Seyler 347 (1993) 166
    • (1993) Biol Chem Hoppe-Seyler , vol.347 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 15
    • 27444438252 scopus 로고    scopus 로고
    • Solvent constraints on the property space of acetylcholine. II. Ordered media
    • Vistoli G., Pedretti A., and Testa B. Solvent constraints on the property space of acetylcholine. II. Ordered media. J Med Chem 48 (2005) 6926-6935
    • (2005) J Med Chem , vol.48 , pp. 6926-6935
    • Vistoli, G.1    Pedretti, A.2    Testa, B.3
  • 18
    • 4143057296 scopus 로고    scopus 로고
    • Structures of Michaelis and product complexes of plant cytokinin dehydrogenase: implications for flavoenzyme catalysis
    • Malito E., Coda A., Bilyeu K.D., Fraaije M.W., and Mattevi A. Structures of Michaelis and product complexes of plant cytokinin dehydrogenase: implications for flavoenzyme catalysis. J Mol Biol 341 (2004) 1237-1249
    • (2004) J Mol Biol , vol.341 , pp. 1237-1249
    • Malito, E.1    Coda, A.2    Bilyeu, K.D.3    Fraaije, M.W.4    Mattevi, A.5
  • 19
    • 34547618240 scopus 로고    scopus 로고
    • The role of hydrophobic interactions in positioning of peripheral proteins in membranes
    • Lomize A.L., Pogozheva I.D., Lomize M.A., and Mosberg H.I. The role of hydrophobic interactions in positioning of peripheral proteins in membranes. BMC Struct Biol 7 (2007) 44
    • (2007) BMC Struct Biol , vol.7 , pp. 44
    • Lomize, A.L.1    Pogozheva, I.D.2    Lomize, M.A.3    Mosberg, H.I.4
  • 20
    • 33744788369 scopus 로고    scopus 로고
    • Homology modeling of human serum carnosinase, a potential medicinal target, and MD simulations of its allosteric activation by citrate
    • Vistoli G., Pedretti A., Cattaneo M., Aldini G., and Testa B. Homology modeling of human serum carnosinase, a potential medicinal target, and MD simulations of its allosteric activation by citrate. J Med Chem 49 (2006) 3269-3277
    • (2006) J Med Chem , vol.49 , pp. 3269-3277
    • Vistoli, G.1    Pedretti, A.2    Cattaneo, M.3    Aldini, G.4    Testa, B.5
  • 21
    • 33645947962 scopus 로고    scopus 로고
    • Functional role of the "aromatic cage" in human monoamine oxidase B: structures and catalytic properties of Tyr435 mutant proteins
    • Li M., Binda C., Mattevi A., and Edmondson D.E. Functional role of the "aromatic cage" in human monoamine oxidase B: structures and catalytic properties of Tyr435 mutant proteins. Biochemistry 45 (2006) 4775-4784
    • (2006) Biochemistry , vol.45 , pp. 4775-4784
    • Li, M.1    Binda, C.2    Mattevi, A.3    Edmondson, D.E.4
  • 23
    • 0031226772 scopus 로고    scopus 로고
    • Empirical scoring functions: I. the development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes
    • Eldridge M., Murray C., Auton T., Paolini G., and Mee R. Empirical scoring functions: I. the development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes. J Comp-Aided Mol Des 11 (1997) 425-445
    • (1997) J Comp-Aided Mol Des , vol.11 , pp. 425-445
    • Eldridge, M.1    Murray, C.2    Auton, T.3    Paolini, G.4    Mee, R.5
  • 24
    • 33749045445 scopus 로고    scopus 로고
    • Amyloid excess in Alzheimer's disease: what is cholesterol to be blamed for?
    • Ledesma M.D., and Dotti C.G. Amyloid excess in Alzheimer's disease: what is cholesterol to be blamed for?. FEBS Lett 580 (2006) 5525-5532
    • (2006) FEBS Lett , vol.580 , pp. 5525-5532
    • Ledesma, M.D.1    Dotti, C.G.2
  • 26
    • 33845207090 scopus 로고    scopus 로고
    • Can statins put the brakes on Alzheimer's disease?
    • Whitfield J.F. Can statins put the brakes on Alzheimer's disease?. Expert Opin Investig Drugs 15 (2006) 1479-1485
    • (2006) Expert Opin Investig Drugs , vol.15 , pp. 1479-1485
    • Whitfield, J.F.1
  • 27
    • 13244272410 scopus 로고    scopus 로고
    • Structural membrane alterations in Alzheimer brains found to be associated with regional disease development; increased density of gangliosides GM1 and GM2 and loss of cholesterol in detergent-resistant membrane domains
    • Molander-Melin M., Blennow K., Bogdanovic N., Dellheden B., Mansson J.E., and Fredman P. Structural membrane alterations in Alzheimer brains found to be associated with regional disease development; increased density of gangliosides GM1 and GM2 and loss of cholesterol in detergent-resistant membrane domains. J Neurochem 92 (2005) 171-182
    • (2005) J Neurochem , vol.92 , pp. 171-182
    • Molander-Melin, M.1    Blennow, K.2    Bogdanovic, N.3    Dellheden, B.4    Mansson, J.E.5    Fredman, P.6
  • 28
    • 14844304305 scopus 로고    scopus 로고
    • Oxidation of cholesterol by amyloid precursor protein and beta-amyloid peptide
    • Nelson T.J., and Alkon D.L. Oxidation of cholesterol by amyloid precursor protein and beta-amyloid peptide. J Biol Chem 280 (2005) 7377-7387
    • (2005) J Biol Chem , vol.280 , pp. 7377-7387
    • Nelson, T.J.1    Alkon, D.L.2
  • 29
    • 1842528400 scopus 로고    scopus 로고
    • Convergence of atherosclerosis and Alzheimer's disease: inflammation, cholesterol, and misfolded proteins
    • Casserly I., and Topol E. Convergence of atherosclerosis and Alzheimer's disease: inflammation, cholesterol, and misfolded proteins. Lancet 363 (2004) 1139-1146
    • (2004) Lancet , vol.363 , pp. 1139-1146
    • Casserly, I.1    Topol, E.2
  • 30
    • 12344270987 scopus 로고    scopus 로고
    • What's so special about cholesterol?
    • Mouritsen O.G., and Zuckermann M.J. What's so special about cholesterol?. Lipids 39 (2004) 1101-1113
    • (2004) Lipids , vol.39 , pp. 1101-1113
    • Mouritsen, O.G.1    Zuckermann, M.J.2
  • 31
    • 33645299023 scopus 로고    scopus 로고
    • The involvement of lipid rafts in Alzheimer's disease
    • Cordy J.M., Hooper N.M., and Turner A.J. The involvement of lipid rafts in Alzheimer's disease. Mol Membr Biol 23 (2006) 111-122
    • (2006) Mol Membr Biol , vol.23 , pp. 111-122
    • Cordy, J.M.1    Hooper, N.M.2    Turner, A.J.3
  • 32
    • 33747821467 scopus 로고    scopus 로고
    • Lovastatin modulates increased cholesterol and oxysterol levels and has a neuroprotective effect on rat hippocampal neurons after kainate injury
    • He X., Jenner A.M., Ong W.Y., Farooqui A.A., and Patel S.C. Lovastatin modulates increased cholesterol and oxysterol levels and has a neuroprotective effect on rat hippocampal neurons after kainate injury. J Neuropathol Exp Neurol 65 (2006) 652-663
    • (2006) J Neuropathol Exp Neurol , vol.65 , pp. 652-663
    • He, X.1    Jenner, A.M.2    Ong, W.Y.3    Farooqui, A.A.4    Patel, S.C.5
  • 33
    • 33748249320 scopus 로고    scopus 로고
    • Structures of biologically active oxysterols determine their differential effects on phospholipid membranes
    • Massey J.B., and Pownall H.J. Structures of biologically active oxysterols determine their differential effects on phospholipid membranes. Biochemistry 45 (2006) 10747-10758
    • (2006) Biochemistry , vol.45 , pp. 10747-10758
    • Massey, J.B.1    Pownall, H.J.2
  • 34
    • 31444454174 scopus 로고    scopus 로고
    • The role of seladin-1/DHCR24 in cholesterol biosynthesis, APP processing and A beta generation in vivo
    • Crameri A., Biondi E., Kuehnle K., Lutjohann D., Thelen K.M., Perga S., et al. The role of seladin-1/DHCR24 in cholesterol biosynthesis, APP processing and A beta generation in vivo. EMBO J 25 (2006) 432-443
    • (2006) EMBO J , vol.25 , pp. 432-443
    • Crameri, A.1    Biondi, E.2    Kuehnle, K.3    Lutjohann, D.4    Thelen, K.M.5    Perga, S.6
  • 36
    • 12844278861 scopus 로고    scopus 로고
    • 3beta-hydroxysterol Delta7-reductase and the Smith-Lemli-Opitz syndrome
    • Correa-Cerro L.S., and Porter F.D. 3beta-hydroxysterol Delta7-reductase and the Smith-Lemli-Opitz syndrome. Mol Genet Metab 84 (2005) 112-126
    • (2005) Mol Genet Metab , vol.84 , pp. 112-126
    • Correa-Cerro, L.S.1    Porter, F.D.2
  • 37
    • 0034634393 scopus 로고    scopus 로고
    • How do substrates enter and products exit the buried active site of cytochrome P450cam? 1. Random expulsion molecular dynamics investigation of ligand access channels and mechanisms
    • Ludemann S.K., Lounnas V., and Wade R.C. How do substrates enter and products exit the buried active site of cytochrome P450cam? 1. Random expulsion molecular dynamics investigation of ligand access channels and mechanisms. J Mol Biol 303 (2000) 797-811
    • (2000) J Mol Biol , vol.303 , pp. 797-811
    • Ludemann, S.K.1    Lounnas, V.2    Wade, R.C.3
  • 38
    • 0034634391 scopus 로고    scopus 로고
    • How do substrates enter and products exit the buried active site of cytochrome P450cam? 2. Steered molecular dynamics and adiabatic mapping of substrate pathways
    • Ludemann S.K., Lounnas V., and Wade R.C. How do substrates enter and products exit the buried active site of cytochrome P450cam? 2. Steered molecular dynamics and adiabatic mapping of substrate pathways. J Mol Biol 303 (2000) 813-830
    • (2000) J Mol Biol , vol.303 , pp. 813-830
    • Ludemann, S.K.1    Lounnas, V.2    Wade, R.C.3
  • 39
    • 33751218931 scopus 로고    scopus 로고
    • Unbinding of retinoic acid from the retinoic acid receptor by random expulsion molecular dynamics
    • Carlsson P., Burendahl S., and Nilsson L. Unbinding of retinoic acid from the retinoic acid receptor by random expulsion molecular dynamics. Biophys J 91 (2006) 3151-3161
    • (2006) Biophys J , vol.91 , pp. 3151-3161
    • Carlsson, P.1    Burendahl, S.2    Nilsson, L.3
  • 40
    • 33749551900 scopus 로고    scopus 로고
    • Odorant binding and conformational dynamics in the odorant-binding protein
    • Hajjar E., Perahia D., Debat H., Nespoulous C., and Robert C.H. Odorant binding and conformational dynamics in the odorant-binding protein. J Mol Biol 281 (2006) 29929-29937
    • (2006) J Mol Biol , vol.281 , pp. 29929-29937
    • Hajjar, E.1    Perahia, D.2    Debat, H.3    Nespoulous, C.4    Robert, C.H.5
  • 41
    • 0347093512 scopus 로고    scopus 로고
    • Role of histidine-85 in the catalytic mechanism of thymidine phosphorylase as assessed by targeted molecular dynamics simulations and quantum mechanical calculations
    • Mendieta J., Martin-Santamaria S., Priego E.M., Balzarini J., Camarasa M.J., Perez-Perez M.J., et al. Role of histidine-85 in the catalytic mechanism of thymidine phosphorylase as assessed by targeted molecular dynamics simulations and quantum mechanical calculations. Biochemistry 43 (2004) 405-414
    • (2004) Biochemistry , vol.43 , pp. 405-414
    • Mendieta, J.1    Martin-Santamaria, S.2    Priego, E.M.3    Balzarini, J.4    Camarasa, M.J.5    Perez-Perez, M.J.6
  • 42
    • 43649087888 scopus 로고    scopus 로고
    • Kuehnle K, Crameri A, Kälin RE, Luciani P, Benvenuti S, Peri A, et al. Pro-survival effect of DHCR24/seladin-1 in an acute and a chronic response to oxidative stress. Mol Cell Biol November 2007 [Epub ahead of print].
    • Kuehnle K, Crameri A, Kälin RE, Luciani P, Benvenuti S, Peri A, et al. Pro-survival effect of DHCR24/seladin-1 in an acute and a chronic response to oxidative stress. Mol Cell Biol November 2007 [Epub ahead of print].


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