메뉴 건너뛰기




Volumn 28, Issue 4, 2009, Pages 305-312

Structural features and dynamics properties of human apolipoprotein A-I in a model of synthetic HDL

Author keywords

Essential dynamics; Lipoprotein; Molecular docking; Molecular dynamics; Molecular modeling

Indexed keywords

AMPHIPATHIC; ANTI-ATHEROGENIC ACTIVITIES; APOLIPOPROTEIN A-I; APOLIPOPROTEINS; DIRECT VISUALIZATION; DRIVING FORCES; DYNAMIC BEHAVIORS; ESSENTIAL DYNAMICS; EXPERIMENTAL APPROACHES; HIGH-DENSITY LIPOPROTEINS; LIPOPROTEIN; MICROSCOPY TECHNIQUE; MOLECULAR DOCKING; MOLECULAR DYNAMICS SIMULATIONS; MOLECULAR MODELS; OUT-OF-PLANE; PHOSPHATIDYLCHOLINE; PROTEIN CHAINS; PROTEIN COMPONENTS; RELATIVE ROTATION; SALT BRIDGES; SECONDARY STRUCTURES; STRUCTURAL FEATURE; TERTIARY STRUCTURES; THEORETICAL MODELS;

EID: 70350571206     PISSN: 10933263     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmgm.2009.08.008     Document Type: Article
Times cited : (8)

References (42)
  • 1
    • 0025883538 scopus 로고
    • Reverse cholesterol transport: physiology and pharmacology
    • Franceschini G., Maderna P., and Sirtori C.R. Reverse cholesterol transport: physiology and pharmacology. Atherosclerosis 88 (1991) 99-107
    • (1991) Atherosclerosis , vol.88 , pp. 99-107
    • Franceschini, G.1    Maderna, P.2    Sirtori, C.R.3
  • 4
    • 0023002101 scopus 로고
    • On computer-assisted analysis of biological sequences: proline punctuation, consensus sequences, and apolipoprotein repeats
    • Boguski M.S., Freeman M., Elshourbagy N.A., Taylor J.M., and Gordon J.I. On computer-assisted analysis of biological sequences: proline punctuation, consensus sequences, and apolipoprotein repeats. J. Lipid Res. 27 (1986) 1011-1034
    • (1986) J. Lipid Res. , vol.27 , pp. 1011-1034
    • Boguski, M.S.1    Freeman, M.2    Elshourbagy, N.A.3    Taylor, J.M.4    Gordon, J.I.5
  • 5
    • 0026736891 scopus 로고
    • Conformational analysis of apolipoprotein A-I and E-3 based on primary sequence and circular dichroism
    • Nolte R.T., and Atkinson D. Conformational analysis of apolipoprotein A-I and E-3 based on primary sequence and circular dichroism. Biophys. J. 63 (1992) 1221-1239
    • (1992) Biophys. J. , vol.63 , pp. 1221-1239
    • Nolte, R.T.1    Atkinson, D.2
  • 6
    • 0030732162 scopus 로고    scopus 로고
    • Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation
    • Borhani D.W., Rogers D.P., Engler J.A., and Brouillette C.G. Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation. Proc. Natl. Acad. Sci. U.S.A. 94 (1997) 12291-12296
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 12291-12296
    • Borhani, D.W.1    Rogers, D.P.2    Engler, J.A.3    Brouillette, C.G.4
  • 7
    • 33144485711 scopus 로고    scopus 로고
    • Crystal structure of human apolipoprotein A-I: insights into its protective effect against cardiovascular diseases
    • Ajees A.A., Anantharamaiah G.M., Mishra V.K., Hussain M.M., and Murthy H.M. Crystal structure of human apolipoprotein A-I: insights into its protective effect against cardiovascular diseases. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 2126-2131
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 2126-2131
    • Ajees, A.A.1    Anantharamaiah, G.M.2    Mishra, V.K.3    Hussain, M.M.4    Murthy, H.M.5
  • 8
    • 0015950692 scopus 로고
    • A molecular theory of lipid-protein interactions in the plasma lipoproteins
    • Segrest J.P., Jackson R.L., Morrisett J.D., and Gotto A.M.J. A molecular theory of lipid-protein interactions in the plasma lipoproteins. FEBS Lett. 38 (1974) 247-258
    • (1974) FEBS Lett. , vol.38 , pp. 247-258
    • Segrest, J.P.1    Jackson, R.L.2    Morrisett, J.D.3    Gotto, A.M.J.4
  • 9
    • 0030786781 scopus 로고    scopus 로고
    • Predicting the structure of apolipoprotein A-I in reconstituted high-density lipoprotein disks
    • Phillips J.C., Wriggers W., Li Z., Jonas A., and Schulten K. Predicting the structure of apolipoprotein A-I in reconstituted high-density lipoprotein disks. Biophys. J. 73 (1997) 2337-2346
    • (1997) Biophys. J. , vol.73 , pp. 2337-2346
    • Phillips, J.C.1    Wriggers, W.2    Li, Z.3    Jonas, A.4    Schulten, K.5
  • 11
    • 0032548464 scopus 로고    scopus 로고
    • Structural analysis of apolipoprotein A-I: effects of amino- and carboxy-terminal deletions on the lipid-free structure
    • Rogers D.P., Roberts L.M., Lebowitz J., Engler J.A., and Brouillette C.G. Structural analysis of apolipoprotein A-I: effects of amino- and carboxy-terminal deletions on the lipid-free structure. Biochemistry 37 (1998) 945-955
    • (1998) Biochemistry , vol.37 , pp. 945-955
    • Rogers, D.P.1    Roberts, L.M.2    Lebowitz, J.3    Engler, J.A.4    Brouillette, C.G.5
  • 14
    • 4644356941 scopus 로고    scopus 로고
    • Identification and structural ramifications of a hinge domain in apolipoprotein A-I discoidal high-density lipoproteins of different size
    • Maiorano J.N., Jandacek R.J., Horace E.M., and Davidson W.S. Identification and structural ramifications of a hinge domain in apolipoprotein A-I discoidal high-density lipoproteins of different size. Biochemistry 43 (2004) 11717-11726
    • (2004) Biochemistry , vol.43 , pp. 11717-11726
    • Maiorano, J.N.1    Jandacek, R.J.2    Horace, E.M.3    Davidson, W.S.4
  • 15
    • 27744536041 scopus 로고    scopus 로고
    • Forster resonance energy transfer measurements are consistent with a helical bundle model for lipid-free apolipoprotein A-I
    • Brouillette C.G., Dong W.J., Yang Z.W., Ray M.J., Protasevich I.I., Cheung H.C., and Engler J.A. Forster resonance energy transfer measurements are consistent with a helical bundle model for lipid-free apolipoprotein A-I. Biochemistry 44 (2005) 16413-16425
    • (2005) Biochemistry , vol.44 , pp. 16413-16425
    • Brouillette, C.G.1    Dong, W.J.2    Yang, Z.W.3    Ray, M.J.4    Protasevich, I.I.5    Cheung, H.C.6    Engler, J.A.7
  • 17
    • 0038526303 scopus 로고    scopus 로고
    • ZDOCK: an initial-stage protein-docking algorithm
    • Chen R., Li L., and Weng Z. ZDOCK: an initial-stage protein-docking algorithm. Proteins 52 (2003) 80-87
    • (2003) Proteins , vol.52 , pp. 80-87
    • Chen, R.1    Li, L.2    Weng, Z.3
  • 18
    • 3142779088 scopus 로고    scopus 로고
    • Structural features of the inactive and active states of the melanin-concentrating hormone receptors: insights from molecular simulations
    • Vitale R.M., Pedone C., De Benedetti P.G., and Fanelli F. Structural features of the inactive and active states of the melanin-concentrating hormone receptors: insights from molecular simulations. Proteins 56 (2004) 430-448
    • (2004) Proteins , vol.56 , pp. 430-448
    • Vitale, R.M.1    Pedone, C.2    De Benedetti, P.G.3    Fanelli, F.4
  • 20
    • 0030821255 scopus 로고    scopus 로고
    • Reconstituted high-density lipoproteins with a disulfide-linked apolipoprotein A-I dimer: evidence for restricted particle size heterogeneity
    • Calabresi L., Vecchio G., Frigerio F., Vavassori L., Sirtori C.R., and Franceschini G. Reconstituted high-density lipoproteins with a disulfide-linked apolipoprotein A-I dimer: evidence for restricted particle size heterogeneity. Biochemistry 36 (1997) 12428-12433
    • (1997) Biochemistry , vol.36 , pp. 12428-12433
    • Calabresi, L.1    Vecchio, G.2    Frigerio, F.3    Vavassori, L.4    Sirtori, C.R.5    Franceschini, G.6
  • 21
    • 0029633168 scopus 로고
    • GROMACS: a message-passing parallel molecular dynamics implementation
    • Berendsen H.J.C., van der Spoel D., and van Drunen R. GROMACS: a message-passing parallel molecular dynamics implementation. Comp. Phys. Commun. 91 (1995) 43-56
    • (1995) Comp. Phys. Commun. , vol.91 , pp. 43-56
    • Berendsen, H.J.C.1    van der Spoel, D.2    van Drunen, R.3
  • 22
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: a package for molecular simulation and trajectory analysis
    • Lindahl E., Hess B., and van der Spoel D. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Model. 7 (2001) 306-317
    • (2001) J. Mol. Model. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoel, D.3
  • 23
    • 70350566323 scopus 로고    scopus 로고
    • D. van der Spoel, A.R. van Buuren, E. Apol, P.J. Meulenhoff, D.P. Tieleman, A.L.T.M. Sijbers, K.A. Feenstra, E. Lindhal, R. van Drunen, H.J.C. Berendsen, Gromacs User Manual version 3.0, Nijenborgh 4, 9747 AG Groningen, 2001.
    • D. van der Spoel, A.R. van Buuren, E. Apol, P.J. Meulenhoff, D.P. Tieleman, A.L.T.M. Sijbers, K.A. Feenstra, E. Lindhal, R. van Drunen, H.J.C. Berendsen, Gromacs User Manual version 3.0, Nijenborgh 4, 9747 AG Groningen, 2001.
  • 24
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature
    • Berger O., Edholm O., and Jahnig F. Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature. Biophys. J. 72 (1997) 2002-2013
    • (1997) Biophys. J. , vol.72 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jahnig, F.3
  • 26
    • 33846823909 scopus 로고
    • Particle mesh Ewald: an N-log(N) method for Ewald sums in large systems
    • Darden T., York D., and Pedersen L. Particle mesh Ewald: an N-log(N) method for Ewald sums in large systems. J. Chem. Phys. 98 (1993) 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 29
    • 0015230409 scopus 로고
    • Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion
    • Lehrer S.S. Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 10 (1971) 3254-3263
    • (1971) Biochemistry , vol.10 , pp. 3254-3263
    • Lehrer, S.S.1
  • 30
    • 0024523877 scopus 로고
    • Defined apolipoprotein A-I conformations in reconstituted high density lipoprotein discs
    • Jonas A., Kezdy K.E., and Wald H.J. Defined apolipoprotein A-I conformations in reconstituted high density lipoprotein discs. J. Biol. Chem. 264 (1989) 4818-4824
    • (1989) J. Biol. Chem. , vol.264 , pp. 4818-4824
    • Jonas, A.1    Kezdy, K.E.2    Wald, H.J.3
  • 31
    • 0027227795 scopus 로고
    • Apolipoprotein A-I conformation in discoidal particles: evidence for alternate structures
    • Calabresi L., Meng Q.H., Castro G.R., and Marcel Y.L. Apolipoprotein A-I conformation in discoidal particles: evidence for alternate structures. Biochemistry 32 (1993) 6477-6484
    • (1993) Biochemistry , vol.32 , pp. 6477-6484
    • Calabresi, L.1    Meng, Q.H.2    Castro, G.R.3    Marcel, Y.L.4
  • 32
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., and Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22 (1983) 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 35
    • 0025202156 scopus 로고
    • Structure of apolipoprotein A-I in three homogeneous, reconstituted high density lipoprotein particles
    • Wald J.H., Krul E.S., and Jonas A. Structure of apolipoprotein A-I in three homogeneous, reconstituted high density lipoprotein particles. J. Biol. Chem. 265 (1990) 20037-20043
    • (1990) J. Biol. Chem. , vol.265 , pp. 20037-20043
    • Wald, J.H.1    Krul, E.S.2    Jonas, A.3
  • 36
    • 0025648850 scopus 로고
    • Apolipoprotein A-I structure and lipid properties in homogeneous, reconstituted spherical and discoidal high density lipoproteins
    • Jonas A., Wald J.H., Toohill K.L.H., Krul E.S., and Kézdy K.E. Apolipoprotein A-I structure and lipid properties in homogeneous, reconstituted spherical and discoidal high density lipoproteins. J. Biol. Chem. 265 (1990) 22123-22129
    • (1990) J. Biol. Chem. , vol.265 , pp. 22123-22129
    • Jonas, A.1    Wald, J.H.2    Toohill, K.L.H.3    Krul, E.S.4    Kézdy, K.E.5
  • 37
    • 0033029275 scopus 로고    scopus 로고
    • Molecular dynamics on a model for nascent high-density lipoprotein: role of salt bridges
    • Sheldahl C., and Harvey S.C. Molecular dynamics on a model for nascent high-density lipoprotein: role of salt bridges. Biophys. J. 76 (1999) 1190-1198
    • (1999) Biophys. J. , vol.76 , pp. 1190-1198
    • Sheldahl, C.1    Harvey, S.C.2
  • 38
    • 0036926084 scopus 로고    scopus 로고
    • Molecular dynamics simulations on discoidal HDL particles suggest a mechanism for rotation in the apo A-I belt model
    • Klon A.E., Segrest J.P., and Harvey S.C. Molecular dynamics simulations on discoidal HDL particles suggest a mechanism for rotation in the apo A-I belt model. J. Mol. Biol. 324 (2002) 703-721
    • (2002) J. Mol. Biol. , vol.324 , pp. 703-721
    • Klon, A.E.1    Segrest, J.P.2    Harvey, S.C.3
  • 39
    • 0021765682 scopus 로고
    • Structural studies of apolipoprotein A-I/phosphatidylcholine recombinants by high-field proton NMR, nondenaturing gradient gel electrophoresis, and electron microscopy
    • Brouillette C.G., Jones J.L., Ng T.C., Kercret H., Chung B.H., and Segrest J.P. Structural studies of apolipoprotein A-I/phosphatidylcholine recombinants by high-field proton NMR, nondenaturing gradient gel electrophoresis, and electron microscopy. Biochemistry 23 (1984) 359-367
    • (1984) Biochemistry , vol.23 , pp. 359-367
    • Brouillette, C.G.1    Jones, J.L.2    Ng, T.C.3    Kercret, H.4    Chung, B.H.5    Segrest, J.P.6
  • 40
    • 0025868703 scopus 로고
    • The epitopes of apolipoprotein A-I define distinct structural domains including a mobile middle region
    • Marcel Y.L., Provost P.R., Koa H., Raffai E., Dac N.V., Fruchart J.C., and Rassart E. The epitopes of apolipoprotein A-I define distinct structural domains including a mobile middle region. J. Biol. Chem. 266 (1991) 3644-3653
    • (1991) J. Biol. Chem. , vol.266 , pp. 3644-3653
    • Marcel, Y.L.1    Provost, P.R.2    Koa, H.3    Raffai, E.4    Dac, N.V.5    Fruchart, J.C.6    Rassart, E.7
  • 42
    • 0029048822 scopus 로고
    • Properties of an N-terminal proteolytic fragment of apolipoprotein A-I in solution and in reconstituted high density lipoproteins
    • Ji Y., and Jonas A. Properties of an N-terminal proteolytic fragment of apolipoprotein A-I in solution and in reconstituted high density lipoproteins. J. Biol. Chem. 270 (1995) 11290-11297
    • (1995) J. Biol. Chem. , vol.270 , pp. 11290-11297
    • Ji, Y.1    Jonas, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.