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Volumn 48, Issue 5, 2005, Pages 1666-1670

Structure of a synthetic fragment of the LALF protein when bound to lipopolysaccharide

Author keywords

[No Author keywords available]

Indexed keywords

LIMULUS ANTILIPOPOLYSACCHARIDE FACTOR; LIMULUS ANTILIPOPOLYSACCHARIDE FACTOR 14; LIPOPOLYSACCHARIDE; PROTEIN; UNCLASSIFIED DRUG;

EID: 14944342494     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm049217k     Document Type: Article
Times cited : (26)

References (25)
  • 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
  • 3
    • 0035524463 scopus 로고    scopus 로고
    • Peptides neutralizinglipopolysaccharide - Structure and function
    • Pristovsek, P.; Kidric, J. Peptides neutralizinglipopolysaccharide - structure and function. Mini Rev. Med. Chem. 2001, 1, 409-416.
    • (2001) Mini Rev. Med. Chem. , vol.1 , pp. 409-416
    • Pristovsek, P.1    Kidric, J.2
  • 4
    • 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.; Weite, 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    Weite, W.5
  • 5
    • 0034660537 scopus 로고    scopus 로고
    • A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins
    • Ferguson, A. D.; Weite, W.; Hofmann, E.; Lindner, B.; Holst, O. et al. A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins. Structure 2000, 8, 585-592.
    • (2000) Structure , vol.8 , pp. 585-592
    • Ferguson, A.D.1    Weite, W.2    Hofmann, E.3    Lindner, B.4    Holst, O.5
  • 6
    • 0027171383 scopus 로고
    • Crystal structure of an endotoxin-neutralizing protein from the horeshoe crab, Limulus anti-LPS factor, at 1.5 a 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 A 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
    • 3142689915 scopus 로고    scopus 로고
    • The search for molecular determinants of LPS inhibition by proteins and peptides
    • Pristovsek, P.; Kidric, J. The search for molecular determinants of LPS inhibition by proteins and peptides. Curr. Topics Med. Chem. 2004, 4, 1185-1201.
    • (2004) Curr. Topics Med. Chem. , vol.4 , pp. 1185-1201
    • Pristovsek, P.1    Kidric, J.2
  • 8
    • 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
  • 9
    • 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
    • Pristovsek, P.; Kidric, 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
    • Pristovsek, P.1    Kidric, J.2
  • 10
    • 0029870193 scopus 로고    scopus 로고
    • Titration calorimetric studies to elucidate the specificity of the interactions of polymyxin B with lipopolysaccharides and lipid A
    • Srimal, S.; Surolia, N.; Balasubramanian, S.; Surolia, A. Titration calorimetric studies to elucidate the specificity of the interactions of polymyxin B with lipopolysaccharides and lipid A. Biochem. J. 1996, 315, 679-686.
    • (1996) Biochem. J. , vol.315 , pp. 679-686
    • Srimal, S.1    Surolia, N.2    Balasubramanian, S.3    Surolia, A.4
  • 11
    • 0036289969 scopus 로고    scopus 로고
    • Identification of LPS-binding peptide fragment of MD-2, a toll-receptor accessory protein
    • Mancek, M.; Pristovsek, P.; Jerala, R. Identification of LPS-binding peptide fragment of MD-2, a toll-receptor accessory protein. Biochem. Biophys. Res. Commun. 2002, 292, 880-885.
    • (2002) Biochem. Biophys. Res. Commun. , vol.292 , pp. 880-885
    • Mancek, M.1    Pristovsek, P.2    Jerala, R.3
  • 12
    • 0038101672 scopus 로고    scopus 로고
    • Enhancement of antibacterial and lipopolysaccharide binding activities of a human lactoferrin peptide fragment by the addition of acyl chain
    • Majerle, A.; Kidrič, J.; Jerala, R. Enhancement of antibacterial and lipopolysaccharide binding activities of a human lactoferrin peptide fragment by the addition of acyl chain. J. Antimicrob. Chemother. 2003, 51, 1159-1165.
    • (2003) J. Antimicrob. Chemother. , vol.51 , pp. 1159-1165
    • Majerle, A.1    Kidrič, J.2    Jerala, R.3
  • 13
    • 3142741110 scopus 로고    scopus 로고
    • The structure of endotoxin-neutralizing peptides bound to LPS
    • IOS Press: Amsterdam
    • Pristovšek, P.; Kidrič, J. The structure of endotoxin-neutralizing peptides bound to LPS. Drug discovery and design: medical aspects; IOS Press: Amsterdam, 2002; pp 161-166.
    • (2002) Drug Discovery and Design: Medical Aspects , pp. 161-166
    • Pristovšek, P.1    Kidrič, J.2
  • 14
    • 0029902934 scopus 로고
    • High affinity endotoxin-binding and neutralizing peptides based on the crystal structure of recombinant limulus anti-lipopolysaccharide factor
    • Ried, C.; Wahl, C.; Miethke, T.; Wellnhofer, G.; Landgraf, C. et al. High affinity endotoxin-binding and neutralizing peptides based on the crystal structure of recombinant limulus anti-lipopolysaccharide factor. J. Biol. Chem. 1986, 271, 28120-28127.
    • (1986) J. Biol. Chem. , vol.271 , pp. 28120-28127
    • Ried, C.1    Wahl, C.2    Miethke, T.3    Wellnhofer, G.4    Landgraf, C.5
  • 16
    • 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
  • 17
    • 0033932904 scopus 로고    scopus 로고
    • Accuracy of bound peptide structures determined by exchange transferred nuclear Overhauser data: A simulation study
    • Eisenmesser, E. Z.; Zabellb, A. P. R.; Post, C. B. Accuracy of bound peptide structures determined by exchange transferred nuclear Overhauser data: A simulation study. J. Biomol. NMR 2000, 17, 17-32.
    • (2000) J. Biomol. NMR , vol.17 , pp. 17-32
    • Eisenmesser, E.Z.1    Zabellb, A.P.R.2    Post, C.B.3
  • 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
  • 21
    • 0036535906 scopus 로고    scopus 로고
    • Complexity and simplicity of ligand-macromolecule interactions: The energy landscape perspective
    • Verkhivker, G. M.; Bouzida, D.; Gehlhaar, D. K.; Rejto, P. A.; Freer, S. T. et al. Complexity and simplicity of ligand-macromolecule interactions: the energy landscape perspective. Curr. Opin. Struct. Biol. 2002, 12, 197-203.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 197-203
    • Verkhivker, G.M.1    Bouzida, D.2    Gehlhaar, D.K.3    Rejto, P.A.4    Freer, S.T.5
  • 22
    • 0033762662 scopus 로고    scopus 로고
    • Production of stable isotope enriched antimicrobial peptides in Escherichia coli: An application to the production of a 15N-enriched fragment of lactoferrin
    • Majerle, A.; Kidrič, J.; Jerala, R. Production of stable isotope enriched antimicrobial peptides in Escherichia coli: An application to the production of a 15N-enriched fragment of lactoferrin. J. Biomol. NMR 2000, 18, 145-151.
    • (2000) J. Biomol. NMR , vol.18 , pp. 145-151
    • Majerle, A.1    Kidrič, J.2    Jerala, R.3
  • 23
    • 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
    • 0023769808 scopus 로고
    • Structure and energetics of ligand binding to proteins: Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system
    • Dauber-Ogusthorpe, P.; Roberts, V. A.; Ogusthorpe, D. J.; Wolff, D. J.; Genest, M. et al. Structure and energetics of ligand binding to proteins: Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system. Proteins Struct. Fund. Genet. 1988, 4, 31-47.
    • (1988) Proteins Struct. Fund. Genet. , vol.4 , pp. 31-47
    • Dauber-Ogusthorpe, P.1    Roberts, V.A.2    Ogusthorpe, D.J.3    Wolff, D.J.4    Genest, M.5
  • 25
    • 11644261806 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. et al. Automated Docking Using a Lamarckian Genetic Algorithm and Empirical Binding Free Energy Function. J. Comput. Chem. 1888, 19, 1639-1662.
    • (1888) 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.