메뉴 건너뛰기




Volumn 48, Issue 24, 2005, Pages 7911-7914

Structure of a synthetic fragment of the lipopolysaccharide (LPS) binding protein when bound to LPS and design of a peptidic LPS inhibitor

Author keywords

[No Author keywords available]

Indexed keywords

ARGINYLVALYLGLUTAMYLGLYCYLARGINYLTRYPTOPHYLLYSYLVALYLARGINYLALANYLSERYLPHEN YLALANYLPHENYLALANYLLYSINE; LBP 14; LIPOPOLYSACCHARIDE BINDING PROTEIN; LIPOPOLYSACCHARIDE BINDING PROTEIN INHIBITOR; PROTEIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 28144454203     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm050762a     Document Type: Article
Times cited : (17)

References (26)
  • 1
    • 0038447123 scopus 로고    scopus 로고
    • Receptors, mediators, and mechanisms involved in bacterial sepsis and septic shock
    • Van Amersfoort, E. S.; Van Berkel, T. J.; Kuiper, J. Receptors, mediators, and mechanisms involved in bacterial sepsis and septic shock. Clin. Microbiol. Rev. 2003, 16, 379-414.
    • (2003) Clin. Microbiol. Rev. , vol.16 , pp. 379-414
    • Van Amersfoort, E.S.1    Van Berkel, T.J.2    Kuiper, J.3
  • 5
    • 3142689915 scopus 로고    scopus 로고
    • The search for molecular determinants of LPS inhibition by proteins and peptides
    • Pristovšek, P.; Kidrič, J. The search for molecular determinants of LPS inhibition by proteins and peptides. Curr. Top. Med. Chem. 2004, 4, 1185-1201.
    • (2004) Curr. Top. Med. Chem. , vol.4 , pp. 1185-1201
    • Pristovšek, P.1    Kidrič, J.2
  • 6
    • 0027171383 scopus 로고
    • Crystal structure of an endotoxin-neutralizing protein from the horeshoe crab, Limulus anti-LPS factor, at 1.5 Å resolution
    • Hoess, A.; Watson, S.; Silber, G. R.; Liddington, R. Crystal structure of an endotoxin-neutralizing protein from the horeshoe crab, Limulus anti-LPS factor, at 1.5 Å resolution EMBO J. 1993, 12, 3351-3356.
    • (1993) EMBO J. , vol.12 , pp. 3351-3356
    • Hoess, A.1    Watson, S.2    Silber, G.R.3    Liddington, R.4
  • 7
    • 0029087339 scopus 로고
    • Peptide derivatives of three distinct lipopolysaccharide binding proteins inhibit lipopolysaccharide-induced tumor necrosos factor-alpha secretion in vitro
    • Battafarano, R. J.; Dahlberg, P. S.; Ratz, C. A.; Johnston, J. W.; Gray, B. H.; Haseman, J. R.; Mayo, K. H.; Dunn, D. L. Peptide derivatives of three distinct lipopolysaccharide binding proteins inhibit lipopolysaccharide-induced tumor necrosos factor-alpha secretion in vitro. Surgery 1995, 118, 318-324.
    • (1995) Surgery , vol.118 , pp. 318-324
    • Battafarano, R.J.1    Dahlberg, P.S.2    Ratz, C.A.3    Johnston, J.W.4    Gray, B.H.5    Haseman, J.R.6    Mayo, K.H.7    Dunn, D.L.8
  • 8
    • 0029028016 scopus 로고
    • Lipopolysaccharide (LPS) neutralizing peptides reveal a lipid a binding site of LPS binding protein
    • Taylor, A. H.; Heavner, G.; Nedelman, M.; Sherris, D.; Brunt, E.; Knight, D.; Ghrayeb, J. Lipopolysaccharide (LPS) neutralizing peptides reveal a lipid A binding site of LPS binding protein. J. Biol. Chem. 1995, 270, 17934-17938.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17934-17938
    • Taylor, A.H.1    Heavner, G.2    Nedelman, M.3    Sherris, D.4    Brunt, E.5    Knight, D.6    Ghrayeb, J.7
  • 9
    • 0036233884 scopus 로고    scopus 로고
    • Identification of single amino acid residues essential for the binding of lipopolysaccharide (LPS) to LPS binding protein (LBP) residues 86-99 by using an Ala-scanning library
    • Reyes, O.; Vallespi, M. G.; Garay, H. E.; Cruz, L. J.; Gonzalez, L. J.; Chinea, G.; Buurman, W.; Arana, M. J. Identification of single amino acid residues essential for the binding of lipopolysaccharide (LPS) to LPS binding protein (LBP) residues 86-99 by using an Ala-scanning library. J. Pept. Sci. 2002, 8, 144-50.
    • (2002) J. Pept. Sci. , vol.8 , pp. 144-150
    • Reyes, O.1    Vallespi, M.G.2    Garay, H.E.3    Cruz, L.J.4    Gonzalez, L.J.5    Chinea, G.6    Buurman, W.7    Arana, M.J.8
  • 10
    • 0033524028 scopus 로고    scopus 로고
    • Solution structure of polymyxins B and E and effect of binding to lipopoly-saccharide: An NMR and molecular modelling study
    • Pristovšek, P.; Kidrič, J. Solution structure of polymyxins B and E and effect of binding to lipopoly-saccharide: an NMR and molecular modelling study. J. Med. Chem. 1999, 42, 4606-4613.
    • (1999) J. Med. Chem. , vol.42 , pp. 4606-4613
    • Pristovšek, P.1    Kidrič, J.2
  • 11
    • 20444505207 scopus 로고    scopus 로고
    • Structural origin of endotoxin neutralization and antimicrobial activity of a lactoferrin-based peptide
    • Japelj, B.; Pristovšek, P.; Majerle, A.; Jerala, R. Structural origin of endotoxin neutralization and antimicrobial activity of a lactoferrin-based peptide. J. Biol. Chem. 2005, 280, 16955-16961.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16955-16961
    • Japelj, B.1    Pristovšek, P.2    Majerle, A.3    Jerala, R.4
  • 12
    • 14944342494 scopus 로고    scopus 로고
    • Structure of a synthetic fragment of the LALF protein when bound to lipopolysaccharide
    • Pristovšek, P.; Feher, K.; Szilagyi, L.; Kidrič, J. Structure of a synthetic fragment of the LALF protein when bound to lipopolysaccharide. J. Med. Chem. 2005, 48, 1666-1670.
    • (2005) J. Med. Chem. , vol.48 , pp. 1666-1670
    • Pristovšek, P.1    Feher, K.2    Szilagyi, L.3    Kidrič, J.4
  • 13
    • 0000393431 scopus 로고
    • Theory and applications of the transferred nuclear Overhauser effect to the study of the conformations of small ligands bound to proteins
    • Clore, G. M.; Gronenborn, A. M. Theory and applications of the transferred nuclear Overhauser effect to the study of the conformations of small ligands bound to proteins. J. Magn. Reson. 1982, 48, 402-417.
    • (1982) J. Magn. Reson. , vol.48 , pp. 402-417
    • Clore, G.M.1    Gronenborn, A.M.2
  • 15
    • 85044009883 scopus 로고    scopus 로고
    • Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution
    • Beamer, L. J.; Carroll, S. F.; Eisenberg, D. Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution. Science 1997, 76, 1861-1864.
    • (1997) Science , vol.76 , pp. 1861-1864
    • Beamer, L.J.1    Carroll, S.F.2    Eisenberg, D.3
  • 16
    • 84903421873 scopus 로고    scopus 로고
    • Three-dimensional structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin
    • Hwang, P. M.; Zhou, N.; Shan, X.; Arrowsmith, C. H.; Vogel, H. J. Three-dimensional structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin. Biochemistry 1998, 37, 4288-4298.
    • (1998) Biochemistry , vol.37 , pp. 4288-4298
    • Hwang, P.M.1    Zhou, N.2    Shan, X.3    Arrowsmith, C.H.4    Vogel, H.J.5
  • 17
    • 0141987859 scopus 로고    scopus 로고
    • Exchange-transferred NOE spectroscopy and bound ligand structure determination
    • Post, C. B. Exchange-transferred NOE spectroscopy and bound ligand structure determination. Curr. Opin. Struct. Biol. 2003, 13, 581-588.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 581-588
    • Post, C.B.1
  • 18
    • 0037189894 scopus 로고    scopus 로고
    • Epitope mapping of ligand-receptor interactions by diffusion NMR
    • Yan, J.; Kline, A. D.; Mo, H.; Zartler, E. R.; Shapiro, M. J. Epitope mapping of ligand-receptor interactions by diffusion NMR. J. Am. Chem. Soc. 2002, 124, 9984-9985.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9984-9985
    • Yan, J.1    Kline, A.D.2    Mo, H.3    Zartler, E.R.4    Shapiro, M.J.5
  • 19
    • 0037083321 scopus 로고    scopus 로고
    • Docking multiple conformations of a flexible ligand into a protein binding site using NMR restraints
    • Zabell, A. P.; Post, C. B. Docking multiple conformations of a flexible ligand into a protein binding site using NMR restraints. Proteins 2002, 46, 295-307.
    • (2002) Proteins , vol.46 , pp. 295-307
    • Zabell, A.P.1    Post, C.B.2
  • 20
    • 0037262054 scopus 로고    scopus 로고
    • Ligand-protein docking: Cancer research at the interface between biology and chemistry
    • Glen, R. C.; Allen, S. C. Ligand-protein docking: cancer research at the interface between biology and chemistry. Curr. Med. Chem. 2003, 10, 763-767.
    • (2003) Curr. Med. Chem. , vol.10 , pp. 763-767
    • Glen, R.C.1    Allen, S.C.2
  • 22
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert, P.; Mumenthaler, C.; Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 1997, 273, 283-298.
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 24
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson, A. D.; Hofmann, E.; Coulton, J. W.; Diederichs, K.; Welte, W. Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science 1998, 282, 2215-2220.
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 25
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and empirical binding free energy function
    • Morris, G. M.; Goodsell, D. S.; Halliday, R. S.; Huey, R.; Hart, W. E.; Belew, R. K.; Olson, A. J. Automated docking using a Lamarckian genetic algorithm and empirical binding free energy function. J. Comput. Chem. 1998, 19, 1639-1662.
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 26
    • 28144438715 scopus 로고    scopus 로고
    • In vitro trials for discovering novel immunomodulatory substanced and possibilities for immunointerventions
    • Simčič, S.; Wraber-Herzog, B.; Pristovšek, P.; Sollner Dolenc, M.; Gobec, S.; Urleb, U. In vitro trials for discovering novel immunomodulatory substanced and possibilities for immunointerventions. Med. Razgledi 2004, 43 (Suppl. 5), 15-19.
    • (2004) Med. Razgledi , vol.43 , Issue.SUPPL. 5 , pp. 15-19
    • Simčič, S.1    Wraber-Herzog, B.2    Pristovšek, P.3    Sollner Dolenc, M.4    Gobec, S.5    Urleb, U.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.