메뉴 건너뛰기




Volumn 91, Issue 8, 2006, Pages 3043-3049

A model structure for the heterodimer apoA-IMilano-apoA-II supports its peculiar susceptibility to proteolysis

Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEIN A1; APOLIPOPROTEIN A2; HETERODIMER; HIGH DENSITY LIPOPROTEIN; LEVAO ALPHA PALMITOYLOLEOYL PHOSPHATIDYLCHOLINE; PHOSPHATIDYLCHOLINE; UNCLASSIFIED DRUG;

EID: 33749529900     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.085886     Document Type: Article
Times cited : (13)

References (41)
  • 1
    • 0025883538 scopus 로고
    • Reverse cholesterol transport: Physiology and pharmacology
    • Franceschini, G., P. Maderna, and C. R. Sirtori. 1991. Reverse cholesterol transport: physiology and pharmacology. Atherosclerosis. 88:99-107.
    • (1991) Atherosclerosis , vol.88 , pp. 99-107
    • Franceschini, G.1    Maderna, P.2    Sirtori, C.R.3
  • 2
    • 0033849918 scopus 로고    scopus 로고
    • Molecular belt models for the apolipoprotein A-I Paris and Milano mutations
    • Klon, A. E., M. K. Jones, J. P. Segrest, and S. C. Harvey. 2000. Molecular belt models for the apolipoprotein A-I Paris and Milano mutations. Biophys. J. 79:1679-1685.
    • (2000) Biophys. J. , vol.79 , pp. 1679-1685
    • Klon, A.E.1    Jones, M.K.2    Segrest, J.P.3    Harvey, S.C.4
  • 3
    • 0022556101 scopus 로고
    • Reconstitution of high-density lipoproteins
    • Jonas, A. 1986. Reconstitution of high-density lipoproteins. Methods Enzymol. 128:553-582.
    • (1986) Methods Enzymol. , vol.128 , pp. 553-582
    • Jonas, A.1
  • 4
    • 0030732162 scopus 로고    scopus 로고
    • Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation
    • Borhani, D. W., D. P. Rogers, J. A. Engler, and C. G. Brouillette. 1997. Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation. Proc. Natl. Acad. Sci. USA. 94:12291-12296.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12291-12296
    • Borhani, D.W.1    Rogers, D.P.2    Engler, J.A.3    Brouillette, C.G.4
  • 5
    • 33144485711 scopus 로고    scopus 로고
    • Crystal structure of human apolipoprotein A-I: Insights into its protective effect against cardiovascular diseases
    • Ajees, A. A., G. M. Anantharamaiah, V. K. Mishra, M. M. Hussain, and H. M. Murthy. 2006. Crystal structure of human apolipoprotein A-I: insights into its protective effect against cardiovascular diseases. Proc. Natl. Acad. Sci. USA. 103:2126-2131.
    • (2006) Proc. Natl. Acad. Sci. USA , 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
  • 6
    • 0036785252 scopus 로고    scopus 로고
    • Structures of apolipoprotein A-II and a lipid-surrogate complex provide insights into apolipoprotein-lipid interactions
    • Kumar, M. S., M. Carson, M. M. Hussain, and H. M. Murthy. 2002. Structures of apolipoprotein A-II and a lipid-surrogate complex provide insights into apolipoprotein-lipid interactions. Biochemistry. 41:11681-11691.
    • (2002) Biochemistry , vol.41 , pp. 11681-11691
    • Kumar, M.S.1    Carson, M.2    Hussain, M.M.3    Murthy, H.M.4
  • 7
    • 0015950692 scopus 로고
    • A molecular theory of lipid-protein interactions in the plasma lipoproteins
    • Segrest, J. P., R. L. Jackson, J. D. Morrisett, and A. M. J. Gotto. 1974. A molecular theory of lipid-protein interactions in the plasma lipoproteins. FEBS Lett. 38:247-258.
    • (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
  • 8
    • 0030786781 scopus 로고    scopus 로고
    • Predicting the structure of apolipoprotein A-I in reconstituted high-density lipoprotein disks
    • Phillips, J. C., W. Wriggers, Z. Li, A. Jonas, and K. Schulten. 1997. Predicting the structure of apolipoprotein A-I in reconstituted high-density lipoprotein disks. Biophys. J. 73:2337-2346.
    • (1997) Biophys. J. , vol.73 , pp. 2337-2346
    • Phillips, J.C.1    Wriggers, W.2    Li, Z.3    Jonas, A.4    Schulten, K.5
  • 10
    • 0035942337 scopus 로고    scopus 로고
    • Arrangement of apolipoprotein A-I in reconstituted high-density lipoprotein disks: An alternative model based on fluorescence resonance energy transfer experiments
    • Tricerri, M. A., A. K. Behling Agree, S. A. Sanchez, J. Bronski, and A. Jonas. 2001. Arrangement of apolipoprotein A-I in reconstituted high-density lipoprotein disks: an alternative model based on fluorescence resonance energy transfer experiments. Biochemistry. 40:5065-5074.
    • (2001) Biochemistry , vol.40 , pp. 5065-5074
    • Tricerri, M.A.1    Behling Agree, A.K.2    Sanchez, S.A.3    Bronski, J.4    Jonas, A.5
  • 12
    • 0033029275 scopus 로고    scopus 로고
    • Molecular dynamics on a model for nascent high-density lipoprotein: Role of salt bridges
    • Sheldahl, C., and S. C. Harvey. 1999. Molecular dynamics on a model for nascent high-density lipoprotein: role of salt bridges. Biophys. J. 76:1190-1198.
    • (1999) Biophys. J. , vol.76 , pp. 1190-1198
    • Sheldahl, C.1    Harvey, S.C.2
  • 13
    • 0019226420 scopus 로고
    • M Apo protein: Decreased high density lipoprotein levels with significant lipoprotein modifications and without clinical atherosclerosis in an Italian family
    • M Apo protein: decreased high density lipoprotein levels with significant lipoprotein modifications and without clinical atherosclerosis in an Italian family. J. Clin. Invest. 66:892-900.
    • (1980) J. Clin. Invest. , vol.66 , pp. 892-900
    • Franceschini, G.1    Sirtori, C.R.2    Capurso, A.3    Weisgraber, K.H.4    Mahley, R.W.5
  • 20
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 21
    • 0020490523 scopus 로고
    • Micellar complexes of human apolipoprotein A-I with phosphatidylcholines and cholesterol prepared from cholate-lipid dispersions
    • Matz, C. E., and A. Jonas. 1982. Micellar complexes of human apolipoprotein A-I with phosphatidylcholines and cholesterol prepared from cholate-lipid dispersions. J. Biol. Chem. 257:4535-4540.
    • (1982) J. Biol. Chem. , vol.257 , pp. 4535-4540
    • Matz, C.E.1    Jonas, A.2
  • 22
    • 0018118041 scopus 로고
    • Circular dichroic analysis of protein conformation: Inclusion of the R-turns
    • Chang, C. T., C. S. Wu, and J. T. Yang. 1978. Circular dichroic analysis of protein conformation: inclusion of the R-turns. Anal. Biochem. 91:13-31.
    • (1978) Anal. Biochem. , vol.91 , pp. 13-31
    • Chang, C.T.1    Wu, C.S.2    Yang, J.T.3
  • 23
    • 0038526303 scopus 로고    scopus 로고
    • ZDOCK: An initial-stage protein-docking algorithm
    • Chen, R., L. Li, and Z. Weng. 2003. ZDOCK: an initial-stage protein-docking algorithm. Proteins. 52:80-87.
    • (2003) Proteins , vol.52 , pp. 80-87
    • Chen, R.1    Li, L.2    Weng, Z.3
  • 25
    • 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., C. Pedone, P. G. De Benedetti, and F. Fanelli. 2004. Structural features of the inactive and active states of the melanin-concentrating hormone receptors: insights from molecular simulations. Proteins. 56:430-448.
    • (2004) Proteins , vol.56 , pp. 430-448
    • Vitale, R.M.1    Pedone, C.2    De Benedetti, P.G.3    Fanelli, F.4
  • 26
    • 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., G. Vecchio, F. Frigerio, L. Vavassori, C. R. Sirtori, and G. Franceschini. 1997. Reconstituted high-density lipoproteins with a disulfide-linked apolipoprotein A-I dimer: evidence for restricted particle size heterogeneity. Biochemistry. 36:12428-12433.
    • (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
  • 27
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature
    • Berger, O., O. Edholm, and F. Jahnig. 1997. Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature. Biophys. J. 72:2002-2013.
    • (1997) Biophys. J. , vol.72 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jahnig, F.3
  • 28
    • 0030239753 scopus 로고    scopus 로고
    • Algorithms for finding the axis of a helix: Fast rotational and parametric leastsquares methods
    • Christopher, J. A., R. Swanson, and T. O. Baldwin. 1996. Algorithms for finding the axis of a helix: fast rotational and parametric leastsquares methods. Comput. Chem. 20:339-345.
    • (1996) Comput. Chem. , vol.20 , pp. 339-345
    • Christopher, J.A.1    Swanson, R.2    Baldwin, T.O.3
  • 29
    • 21244497735 scopus 로고    scopus 로고
    • Penetratin-membrane association: W48/R52/W56 shield the peptide from the aqueous phase
    • Lensink, M. F., B. Christiaens, J. Vandekerckhove, A. Prochiantz, and M. Rosseneu. 2005. Penetratin-membrane association: W48/R52/W56 shield the peptide from the aqueous phase. Biophys. J. 88:939-952.
    • (2005) Biophys. J. , vol.88 , pp. 939-952
    • Lensink, M.F.1    Christiaens, B.2    Vandekerckhove, J.3    Prochiantz, A.4    Rosseneu, M.5
  • 31
    • 0030900911 scopus 로고    scopus 로고
    • Structural analysis of apolipoprotein A-I: Limited proteolysis of methionine-reduced and -oxidized lipid-free and lipid-bound human apo A-I
    • Roberts, L. M., M. J. Ray, T.-W. Shih, E. Hayden, M. M. Reader, and C. G. Brouillette. 1997. Structural analysis of apolipoprotein A-I: limited proteolysis of methionine-reduced and -oxidized lipid-free and lipid-bound human apo A-I. Biochemistry. 36:7615-7624.
    • (1997) Biochemistry , vol.36 , pp. 7615-7624
    • Roberts, L.M.1    Ray, M.J.2    Shih, T.-W.3    Hayden, E.4    Reader, M.M.5    Brouillette, C.G.6
  • 32
    • 0025121944 scopus 로고
    • Pre-β high density lipoprotein: Unique disposition of apolipoprotein A-I increases susceptibility to proteolysis
    • Kunitake, S. T., G. C. Chen, S. F. Kung, J. W. Schilling, D. A. Hardman, and J. P. Kane. 1990. Pre-β high density lipoprotein: unique disposition of apolipoprotein A-I increases susceptibility to proteolysis. Arteriosclerosis. 10:25-30.
    • (1990) Arteriosclerosis , vol.10 , pp. 25-30
    • Kunitake, S.T.1    Chen, G.C.2    Kung, S.F.3    Schilling, J.W.4    Hardman, D.A.5    Kane, J.P.6
  • 33
    • 0027219389 scopus 로고
    • Structural and functional domains of apolipoprotein A-I within high density lipoproteins
    • Dalton, M. B., and J. B. Swaney. 1993. Structural and functional domains of apolipoprotein A-I within high density lipoproteins. J. Biol. Chem. 268:19274-19283.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19274-19283
    • Dalton, M.B.1    Swaney, J.B.2
  • 35
    • 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 A. Jonas. 1995. Properties of an N-terminal proteolytic fragment of apolipoprotein A-I in solution and in reconstituted high density lipoproteins. J. Biol. Chem. 270:11290-11297.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11290-11297
    • Ji, Y.1    Jonas, A.2
  • 37
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and C. Sander. 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
  • 38
    • 11244346546 scopus 로고    scopus 로고
    • Molecular dynamics simulations of discoidal bilayers assembled from truncated human lipoproteins
    • Shih, A. Y., I. G. Denisov, J. C. Phillips, S. G. Sligar, and K. Schulten. 2005. Molecular dynamics simulations of discoidal bilayers assembled from truncated human lipoproteins. Biophys. J. 88:548-556.
    • (2005) Biophys. J. , vol.88 , pp. 548-556
    • Shih, A.Y.1    Denisov, I.G.2    Phillips, J.C.3    Sligar, S.G.4    Schulten, K.5
  • 39
    • 0043007514 scopus 로고    scopus 로고
    • Self-assembly of discoidal phospholipid bilayer nanoparticles with membrane scaffold proteins
    • Bayburt, T. H., Y. V. Grinkova, and S. G. Sligar. 2002. Self-assembly of discoidal phospholipid bilayer nanoparticles with membrane scaffold proteins. Nano Lett. 2:853-856.
    • (2002) Nano Lett. , vol.2 , pp. 853-856
    • Bayburt, T.H.1    Grinkova, Y.V.2    Sligar, S.G.3
  • 40
    • 1642382983 scopus 로고    scopus 로고
    • Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size
    • Denisov, I. G., Y. V. Grinkova, A. A. Lazarides, and S. G. Sligar. 2004. Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size. J. Am. Chem. Soc. 126:3477-3487.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3477-3487
    • Denisov, I.G.1    Grinkova, Y.V.2    Lazarides, A.A.3    Sligar, S.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.