메뉴 건너뛰기




Volumn 6, Issue 7, 1998, Pages 895-909

The structural basis of lipid interactions in lipovitellin, a soluble lipoprotein

Author keywords

Apolipoprotein B; Lipoprotein; Lipovitellin; Microsomal triglyceride transfer protein; X ray crystallography

Indexed keywords

PETROMYZONTIDAE;

EID: 0032527992     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00091-4     Document Type: Article
Times cited : (143)

References (53)
  • 1
    • 0021764704 scopus 로고
    • Preparation of single crystals of a yolk lipoprotein
    • Meininger, T., Raag, R., Roderick, S. & Banaszak, L.J. (1984). Preparation of single crystals of a yolk lipoprotein. J. mol. Biol. 179, 759-764.
    • (1984) J. Mol. Biol. , vol.179 , pp. 759-764
    • Meininger, T.1    Raag, R.2    Roderick, S.3    Banaszak, L.J.4
  • 2
    • 0024278397 scopus 로고
    • Structure of the lamprey yolk lipid-protein complex lipovitellin-phosvitin at 2.8 A resolution
    • Raag, R. Appelt, K., Xuong, N.-H. & Banaszak, L. (1988). Structure of the lamprey yolk lipid-protein complex lipovitellin-phosvitin at 2.8 A resolution. J. Mol. Biol. 200, 553-569.
    • (1988) J. Mol. Biol. , vol.200 , pp. 553-569
    • Raag, R.1    Appelt, K.2    Xuong, N.-H.3    Banaszak, L.4
  • 4
    • 0026673549 scopus 로고
    • Sequence of lamprey vitellogenin: Implications for the lipovitellin crystal structure
    • Sharrock, W.J., et al., & Banaszak, L. (1992). Sequence of lamprey vitellogenin: implications for the lipovitellin crystal structure. J. Mol. Biol. 226, 903-907.
    • (1992) J. Mol. Biol. , vol.226 , pp. 903-907
    • Sharrock, W.J.1    Banaszak, L.2
  • 6
    • 0017712492 scopus 로고
    • Lipid and polypeptide components of the crystalline yolk system from Xenopus laevis
    • Ohlendorf, D.H., Barbarash, G.R., Trout, A., Kent, C. & Banaszak, L.J. (1977). Lipid and polypeptide components of the crystalline yolk system from Xenopus laevis. J. Biol. Chem. 252, 7992-8001.
    • (1977) J. Biol. Chem. , vol.252 , pp. 7992-8001
    • Ohlendorf, D.H.1    Barbarash, G.R.2    Trout, A.3    Kent, C.4    Banaszak, L.J.5
  • 7
    • 0021779490 scopus 로고
    • Induction, isolation and a characterization of the lipid content of plasma vitellogenin from two salmon species: Rainbow trout (Salmo gairdneri) and sea trout (Salmo trutta)
    • Norberg, B. & Haux, C. (1985). Induction, isolation and a characterization of the lipid content of plasma vitellogenin from two salmon species: rainbow trout (Salmo gairdneri) and sea trout (Salmo trutta). Comp. Biochem. Physiol. B 81, 869-876.
    • (1985) Comp. Biochem. Physiol. B , vol.81 , pp. 869-876
    • Norberg, B.1    Haux, C.2
  • 8
    • 0029096711 scopus 로고
    • Vitellogenin and lipovitellin: Zinc proteins of Xenopus laevis oocytes
    • Montorzi, M., Falchuk, K.H. & Vallee, B.L. (1995). Vitellogenin and lipovitellin: zinc proteins of Xenopus laevis oocytes. Biochemistry 34, 10851-10858.
    • (1995) Biochemistry , vol.34 , pp. 10851-10858
    • Montorzi, M.1    Falchuk, K.H.2    Vallee, B.L.3
  • 9
    • 0026688272 scopus 로고
    • The location of bound lipid in lipovitellin complex
    • Timmins, P.A., Poliks, B. & Banaszak, L. (1992). The location of bound lipid in lipovitellin complex. Science 257, 652-655.
    • (1992) Science , vol.257 , pp. 652-655
    • Timmins, P.A.1    Poliks, B.2    Banaszak, L.3
  • 10
    • 0023708536 scopus 로고
    • Is vitellogenin an ancestor of apolipoprotein B-100 of human LDL and human lipoprotein lipase?
    • Baker, M.E. (1988). Is vitellogenin an ancestor of apolipoprotein B-100 of human LDL and human lipoprotein lipase? Biochem. J. 255, 1057-1060.
    • (1988) Biochem. J. , vol.255 , pp. 1057-1060
    • Baker, M.E.1
  • 11
    • 0027716370 scopus 로고
    • Abetalipoproteinemia is caused by defects of the gene encoding the 97 kDa subunit of a microsomal triglyceride transfer protein
    • Shoulders, C.C., et al., & Scott, J. (1993). Abetalipoproteinemia is caused by defects of the gene encoding the 97 kDa subunit of a microsomal triglyceride transfer protein. Hum. Mol. Gen. 2, 2109-2116.
    • (1993) Hum. Mol. Gen. , vol.2 , pp. 2109-2116
    • Shoulders, C.C.1    Scott, J.2
  • 12
    • 0028440629 scopus 로고
    • The abetalipoproteinemia gene is a member of the vitellogenin family and encodes an α-helical domain
    • Shoulders, C.C., et al., & Banaszak, L.J. (1994). The abetalipoproteinemia gene is a member of the vitellogenin family and encodes an α-helical domain. Nat. Struct. Biol. 1, 285-286.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 285-286
    • Shoulders, C.C.1    Banaszak, L.J.2
  • 13
    • 0023056989 scopus 로고
    • Complete cDNA and derived protein sequence of human apolipoprotein B-100
    • Knott, TJ., et al., & Scott, J. (1986). Complete cDNA and derived protein sequence of human apolipoprotein B-100. Nucleic Acids Res. 14, 7501-7503.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 7501-7503
    • Knott, T.J.1    Scott, J.2
  • 14
    • 0024289536 scopus 로고
    • Invertebrate vitellogenin is homologous to human von Willebrand factor
    • Baker, M.E. (1988). Invertebrate vitellogenin is homologous to human von Willebrand factor. Biochem. J. 256, 1059-1063.
    • (1988) Biochem. J. , vol.256 , pp. 1059-1063
    • Baker, M.E.1
  • 15
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H.N., Engelbrecht, J., Brunak, S. & von Heijne, G. (1997). Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10, 1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.N.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 16
    • 0020480289 scopus 로고
    • Lipid domains in the crystalline lipovitellin/phosvitin complex: A phosphorus-31 and deuterium nuclear magnetic resonance study
    • Banaszak, L.J. & Seelig, J. (1982). Lipid domains in the crystalline lipovitellin/phosvitin complex: a phosphorus-31 and deuterium nuclear magnetic resonance study. Biochemistry 21, 2436-2443.
    • (1982) Biochemistry , vol.21 , pp. 2436-2443
    • Banaszak, L.J.1    Seelig, J.2
  • 17
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF-a program to identify and analyze structural motifs in proteins
    • Hutchinson, E.G. & Thornton, J.M. (1996). PROMOTIF-a program to identify and analyze structural motifs in proteins. Protein Sci. 5, 212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 18
    • 0028091202 scopus 로고
    • Doughnutshaped structure of a bacterial muramidase revealed by X-ray crystallography
    • Thunnissen, A.-M.W.H., et al., & Dijkstra, B.W. (1994). Doughnutshaped structure of a bacterial muramidase revealed by X-ray crystallography. Nature 367, 750-753.
    • (1994) Nature , vol.367 , pp. 750-753
    • Thunnissen, A.-M.W.H.1    Dijkstra, B.W.2
  • 19
    • 0025860481 scopus 로고
    • Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E
    • Wilson, C., Wardell, M.R., Weisgraber, K.H., Mahley, R.W. & Agard, D.A. (1991). Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E. Science 252, 1817-1822.
    • (1991) Science , vol.252 , pp. 1817-1822
    • Wilson, C.1    Wardell, M.R.2    Weisgraber, K.H.3    Mahley, R.W.4    Agard, D.A.5
  • 20
    • 0026101543 scopus 로고
    • Molecular structure of an apolipoprotein determined at 2.5 Å resolution
    • Breiter, D.R., et al., & Holden, H.M. (1991). Molecular structure of an apolipoprotein determined at 2.5 Å resolution. Biochemistry 30, 603-608.
    • (1991) Biochemistry , vol.30 , pp. 603-608
    • Breiter, D.R.1    Holden, H.M.2
  • 21
    • 0027180507 scopus 로고
    • Verification of protein structures: Patterns of nonbonded atomic interactions
    • Colovos, C. & Yeates, T.O. (1993). Verification of protein structures: patterns of nonbonded atomic interactions. Protein Sci. 2, 1511-1519.
    • (1993) Protein Sci. , vol.2 , pp. 1511-1519
    • Colovos, C.1    Yeates, T.O.2
  • 22
    • 0020480244 scopus 로고
    • Lipid environments in the yolk lipoprotein system. A spin-labeling study of the lipovitellin/phosvitin complex from Xenopus laevis
    • Birrell, G.B., Anderson, P.B., Jost, P.C., Griffith, O.H., Banaszak, L.J. & Seelig, J. (1982). Lipid environments in the yolk lipoprotein system. A spin-labeling study of the lipovitellin/phosvitin complex from Xenopus laevis. Biochemistry 21, 2444-2452.
    • (1982) Biochemistry , vol.21 , pp. 2444-2452
    • Birrell, G.B.1    Anderson, P.B.2    Jost, P.C.3    Griffith, O.H.4    Banaszak, L.J.5    Seelig, J.6
  • 23
    • 0029867027 scopus 로고    scopus 로고
    • X-ray absorption fine structure as a monitor of zinc coordination sites during oogenesis of Xenopus laevis
    • Auld, D.S., Falchuk, K.H., Zhang, K, Montorzi, M. & Vallee, B.L (1996). X-ray absorption fine structure as a monitor of zinc coordination sites during oogenesis of Xenopus laevis. Proc. Natl Acad. Sci. USA 93, 3227-3231.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 3227-3231
    • Auld, D.S.1    Falchuk, K.H.2    Zhang, K.3    Montorzi, M.4    Vallee, B.L.5
  • 24
    • 13144255416 scopus 로고
    • Biliverdin: A component of yolk proteins in Xenopus laevis
    • Redshaw, M.R., Follett, B.K. & Lawes, G.J. (1971). Biliverdin: a component of yolk proteins in Xenopus laevis. Int. J. Biochem. 2, 80-84.
    • (1971) Int. J. Biochem. , vol.2 , pp. 80-84
    • Redshaw, M.R.1    Follett, B.K.2    Lawes, G.J.3
  • 25
    • 0030913589 scopus 로고    scopus 로고
    • Evolution of processes and regulators of lipoprotein synthesis: From birds to mammals
    • Davis, R.A. (1997). Evolution of processes and regulators of lipoprotein synthesis: from birds to mammals. J. Nutr. 127, 795S-800S.
    • (1997) J. Nutr. , vol.127
    • Davis, R.A.1
  • 27
    • 0030070695 scopus 로고    scopus 로고
    • The Caenorhabditis elegans genome project. C. elegans genome consortium
    • Coulson, A. (1996). The Caenorhabditis elegans genome project. C. elegans genome consortium. Biochem. Soc. Trans. 24, 289-291.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 289-291
    • Coulson, A.1
  • 28
    • 0027486706 scopus 로고
    • Mechanism of microsomal trigylceride transfer protein catalyzed lipid transport
    • Atzel, A. & Wetterau, J.R. (1993). Mechanism of microsomal trigylceride transfer protein catalyzed lipid transport. Biochemistry 32, 10444-10500.
    • (1993) Biochemistry , vol.32 , pp. 10444-10500
    • Atzel, A.1    Wetterau, J.R.2
  • 29
    • 0028606834 scopus 로고
    • Identification of two classes of lipid molecules binding sites on the microsomal triglyceride transfer protein
    • Atzel, A. & Wetterau, J.R. (1994). Identification of two classes of lipid molecules binding sites on the microsomal triglyceride transfer protein. Biochemistry 33, 15382-15388.
    • (1994) Biochemistry , vol.33 , pp. 15382-15388
    • Atzel, A.1    Wetterau, J.R.2
  • 30
    • 0025742664 scopus 로고
    • Carboxyl-terminal truncation of apolipoprotein B results in gradual loss of the ability to form buoyant lipoproteins in cultured human and rat liver cell lines
    • Graham, D.L., Knott, T.J., Jones, T.C., Pease, R.J., Pullinger, C.R. & Scott, J. (1991). Carboxyl-terminal truncation of apolipoprotein B results in gradual loss of the ability to form buoyant lipoproteins in cultured human and rat liver cell lines. Biochemistry 30, 5616-5621.
    • (1991) Biochemistry , vol.30 , pp. 5616-5621
    • Graham, D.L.1    Knott, T.J.2    Jones, T.C.3    Pease, R.J.4    Pullinger, C.R.5    Scott, J.6
  • 32
    • 0021764626 scopus 로고
    • Lattice parameters as revealed by electron microscopy and a comparison between lipoprotein crystals from cyclostome eggs formed in vivo and in vitro
    • Lange, R.H. (1984). Lattice parameters as revealed by electron microscopy and a comparison between lipoprotein crystals from cyclostome eggs formed in vivo and in vitro. J. Mol. Biol. 179, 765-768.
    • (1984) J. Mol. Biol. , vol.179 , pp. 765-768
    • Lange, R.H.1
  • 33
    • 0019784255 scopus 로고
    • Pyroglutamic acid: Non-metabolic formation, function in proteins and peptides, and characteristics of the enzymes effecting its removal
    • Abraham, G.N. & Podell, D.N. (1981). Pyroglutamic acid: non-metabolic formation, function in proteins and peptides, and characteristics of the enzymes effecting its removal. Mol. Cell Biochem. 38, 181-190.
    • (1981) Mol. Cell Biochem. , vol.38 , pp. 181-190
    • Abraham, G.N.1    Podell, D.N.2
  • 34
    • 0022325950 scopus 로고
    • Resolution of phase ambiguity in macromolecular crystallography
    • Wang, B.-C. (1985). Resolution of phase ambiguity in macromolecular crystallography. Methods Enzymol. 115, 90-112.
    • (1985) Methods Enzymol. , vol.115 , pp. 90-112
    • Wang, B.-C.1
  • 35
    • 0027677912 scopus 로고
    • A new routine for thinning, editing, and fitting MIR maps using real-space molecular dynamics
    • Levitt, D.G. & Banaszak, L.J. (1993). A new routine for thinning, editing, and fitting MIR maps using real-space molecular dynamics. J. Appl. Cryst. 26, 736-745.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 736-745
    • Levitt, D.G.1    Banaszak, L.J.2
  • 36
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta. Cryst. A 47, 110-119.
    • (1991) Acta. Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 38
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, AT. (1992). The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 39
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R.A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Cryst. A 47, 392-400.
    • (1991) Acta Cryst. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 40
    • 84901961522 scopus 로고
    • Slow-cooling protocols for crystallographic refinement by simulated annealing
    • Brünger, AT., Krukowski, A. & Erickson, J. (1990). Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Cryst. A 46, 585-593.
    • (1990) Acta Cryst. A , vol.46 , pp. 585-593
    • Brünger, A.T.1    Krukowski, A.2    Erickson, J.3
  • 41
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy atom parameters
    • (Wolf, W., Evans, P.R. & Leslie, A.G.W., eds), Science & Engineering Research Council Daresbury Laboratory, Warrington, UK
    • Otwinoski, Z. (1991). Maximum likelihood refinement of heavy atom parameters. In Isomorphous Replacement and Anomalous Scattering (Wolf, W., Evans, P.R. & Leslie, A.G.W., eds), pp. 80-86, Science & Engineering Research Council Daresbury Laboratory, Warrington, UK.
    • (1991) Isomorphous Replacement and Anomalous Scattering , pp. 80-86
    • Otwinoski, Z.1
  • 42
    • 0642288090 scopus 로고
    • Heavy-atom refinement against solvent-flattened phases
    • Cura, V., Krishnaswamy, S. & Podjarny, A.D. (1992). Heavy-atom refinement against solvent-flattened phases. Acta Cryst. A 48, 756-764.
    • (1992) Acta Cryst. A , vol.48 , pp. 756-764
    • Cura, V.1    Krishnaswamy, S.2    Podjarny, A.D.3
  • 43
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 45
    • 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 Cryst. A 42, 140-149.
    • (1986) Acta Cryst. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 46
    • 0002738008 scopus 로고
    • Dictionaries for heteros
    • Kleywegt, G.J. (1995). Dictionaries for heteros. ESFICCP4 Newslett. 31, 45-50.
    • (1995) ESFICCP4 Newslett. , vol.31 , pp. 45-50
    • Kleywegt, G.J.1
  • 47
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of a protein structure
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of a protein structure. J. Appl. Cryst. 26, 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
  • 48
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy, R., Bowie, J.U. & Eisenberg, D. (1992). Assessment of protein models with three-dimensional profiles. Nature 356, 83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 49
    • 0003699451 scopus 로고
    • Biosym/MSI, San Diego, CA
    • Insight II User Guide, (1995). Biosym/MSI, San Diego, CA.
    • (1995) Insight II User Guide
  • 50
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structures: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. & Sander, C. (1983). Dictionary of protein secondary structures: 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
  • 51
    • 0000732609 scopus 로고
    • GRASP: A graphical representation and analysis of surface properties
    • Nicholls, A., Bharadwaj, R. & Honig, B. (1993). GRASP: a graphical representation and analysis of surface properties. Biophys. J. 64, A166.
    • (1993) Biophys. J. , vol.64
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3
  • 52
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G.J. (1993). ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6, 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 53
    • 0027609916 scopus 로고
    • SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules
    • Evans, S.V. (1993). SETOR: hardware-lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11, 134-138.
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.