메뉴 건너뛰기




Volumn 10, Issue 1, 1999, Pages 42-47

NMR spectroscopy in structure-based drug design

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 0032899363     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(99)80008-1     Document Type: Article
Times cited : (47)

References (73)
  • 1
    • 0032146301 scopus 로고    scopus 로고
    • Structure-based drug design
    • Amzel LM Structure-based drug design. Curr Opin Biotechnol. 9:1998;366-369.
    • (1998) Curr Opin Biotechnol , vol.9 , pp. 366-369
    • Amzel, L.M.1
  • 2
    • 0031569368 scopus 로고    scopus 로고
    • Serendipity meets precision: The integration of structure-based drug design and combinatorial chemistry for efficient drug discovery
    • Salemme FR, Spurlino J, Bone R Serendipity meets precision: the integration of structure-based drug design and combinatorial chemistry for efficient drug discovery. Structure. 5:1997;319-324.
    • (1997) Structure , vol.5 , pp. 319-324
    • Salemme, F.R.1    Spurlino, J.2    Bone, R.3
  • 3
    • 0001307841 scopus 로고    scopus 로고
    • NMR spectroscopy as a tool for structure-based drug design
    • A valuable current review of the field describing the basic techniques used to study protein-ligand complexes and their application to a number of specific drug-target systems, including immunophilins, HIV protease, dihydrofolate reductase, matrix metalloproteinases and glycoprotein IIb-IIIa.
    • Stockman BJ NMR spectroscopy as a tool for structure-based drug design. Prog NMR Spectrosc. 33:1998;109-151. A valuable current review of the field describing the basic techniques used to study protein-ligand complexes and their application to a number of specific drug-target systems, including immunophilins, HIV protease, dihydrofolate reductase, matrix metalloproteinases and glycoprotein IIb-IIIa.
    • (1998) Prog NMR Spectrosc , vol.33 , pp. 109-151
    • Stockman, B.J.1
  • 5
    • 0031804609 scopus 로고    scopus 로고
    • Inhibitors of HIV-1 protease: A major success of structure-assisted drug design
    • An informative and critical review of the contributions of crystallography and NMR to the design of HIV protease inhibitors, including several case studies.
    • Wlodawer A, Vondrasek J Inhibitors of HIV-1 protease: a major success of structure-assisted drug design. Annu Rev Biophys Biomol Struct. 27:1998;249-284. An informative and critical review of the contributions of crystallography and NMR to the design of HIV protease inhibitors, including several case studies.
    • (1998) Annu Rev Biophys Biomol Struct , vol.27 , pp. 249-284
    • Wlodawer, A.1    Vondrasek, J.2
  • 7
    • 0029962943 scopus 로고    scopus 로고
    • DNA bending and unwinding associated with actinomycin D antibiotics bound to partially overlapping sites on DNA
    • Chen H, Liu X, Patel DJ DNA bending and unwinding associated with actinomycin D antibiotics bound to partially overlapping sites on DNA. J Mol Biol. 258:1996;457-479.
    • (1996) J Mol Biol , vol.258 , pp. 457-479
    • Chen, H.1    Liu, X.2    Patel, D.J.3
  • 9
    • 0031575419 scopus 로고    scopus 로고
    • 1-DNA complex
    • ••] describe the structures of complexes of two enediyne antitumour antibiotics with cognate oligonucleotides. These structures provide explanations for the observed sequence-specificity of the two compounds, and show how the binding positions the pro-radical centres appropriately for double-strand cleavage.
    • ••] describe the structures of complexes of two enediyne antitumour antibiotics with cognate oligonucleotides. These structures provide explanations for the observed sequence-specificity of the two compounds, and show how the binding positions the pro-radical centres appropriately for double-strand cleavage.
    • (1997) J Mol Biol , vol.265 , pp. 187-201
    • Kumar, R.A.1    Ikemoto, N.2    Patel, D.J.3
  • 11
    • 0030735988 scopus 로고    scopus 로고
    • Solution NMR spectroscopy beyond 25 kDa
    • Kay LE, Gardner KH Solution NMR spectroscopy beyond 25 kDa. Curr Opin Struct Biol. 7:1997;722-731.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 722-731
    • Kay, L.E.1    Gardner, K.H.2
  • 12
    • 0030963093 scopus 로고    scopus 로고
    • Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy
    • Tjandra N, Garrett DS, Gronenborn AM, Bax A, Clore GM Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy. Nat Struct Biol. 4:1997;443-449.
    • (1997) Nat Struct Biol , vol.4 , pp. 443-449
    • Tjandra, N.1    Garrett, D.S.2    Gronenborn, A.M.3    Bax, A.4    Clore, G.M.5
  • 13
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • Describes the use of residual dipolar couplings in proteins partly oriented in a dilute solution of phospholipid bicelles to obtain structural information. This is an important addition to the available methods for obtaining structural information from NMR.
    • Tjandra N, Bax A Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science. 278:1997;1111-1114. Describes the use of residual dipolar couplings in proteins partly oriented in a dilute solution of phospholipid bicelles to obtain structural information. This is an important addition to the available methods for obtaining structural information from NMR.
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 14
    • 0030612833 scopus 로고    scopus 로고
    • 2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • 1H cross-peak in, for example, an HMQC spectrum. This paper describes a method for selecting only the narrowest component, making it possible to obtain sharp lines from large proteins, and thus promising to extend substantially the upper size limit for studying proteins by NMR.
    • 1H cross-peak in, for example, an HMQC spectrum. This paper describes a method for selecting only the narrowest component, making it possible to obtain sharp lines from large proteins, and thus promising to extend substantially the upper size limit for studying proteins by NMR.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12366-12371
    • Peruvshkin, K.1    Riek, R.2    Wider, G.3    Wüthrich, K.4
  • 15
    • 0030778008 scopus 로고    scopus 로고
    • Probing molecular motion by NMR
    • A valuable review describing recent developments in NMR methods for studying internal motion in proteins.
    • Palmer AG III Probing molecular motion by NMR. Curr Opin Struct Biol. 7:1997;732-737. A valuable review describing recent developments in NMR methods for studying internal motion in proteins.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 732-737
    • Palmer A.G. III1
  • 16
    • 0030433170 scopus 로고    scopus 로고
    • Protein dynamics and conformational transitions in allosteric proteins
    • Jardetzky O Protein dynamics and conformational transitions in allosteric proteins. Prog Biophys Mol Biol. 65:1996;171-218.
    • (1996) Prog Biophys Mol Biol , vol.65 , pp. 171-218
    • Jardetzky, O.1
  • 17
    • 0032101346 scopus 로고    scopus 로고
    • Essential spaces defined by NMR structure ensembles and molecular dynamics simulation show significant overlap
    • An informative comparison of the structural ensembles obtained by NMR and by molecular dynamics simulations for two very different systems. The rather surprising conclusion is that the large-scale correlated motions indicated by the two very different methods are quite similar. This lends support to the idea that less well-defined regions of solution structures determined by NMR are likely to be mobile. The comparison also leads to a proposal for an improved selection criterion for inclusion of structures in the 'NMR ensemble' to ensure that amplitudes of motion are better represented.
    • Abseher A, Horstink L, Hilbers CW, Nilges M Essential spaces defined by NMR structure ensembles and molecular dynamics simulation show significant overlap. Proteins Struct Func Genet. 31:1998;370-382. An informative comparison of the structural ensembles obtained by NMR and by molecular dynamics simulations for two very different systems. The rather surprising conclusion is that the large-scale correlated motions indicated by the two very different methods are quite similar. This lends support to the idea that less well-defined regions of solution structures determined by NMR are likely to be mobile. The comparison also leads to a proposal for an improved selection criterion for inclusion of structures in the 'NMR ensemble' to ensure that amplitudes of motion are better represented.
    • (1998) Proteins Struct Func Genet , vol.31 , pp. 370-382
    • Abseher, A.1    Horstink, L.2    Hilbers, C.W.3    Nilges, M.4
  • 18
    • 0031984752 scopus 로고    scopus 로고
    • Pervasive conformational fluctuations on microsecond timescales in a fibronectin type III domain
    • Akke M, Liu J, Cavanagh J, Erickson HP, Palmer AG III Pervasive conformational fluctuations on microsecond timescales in a fibronectin type III domain. Nat Struct Biol. 5:1998;55-59.
    • (1998) Nat Struct Biol , vol.5 , pp. 55-59
    • Akke, M.1    Liu, J.2    Cavanagh, J.3    Erickson, H.P.4    Palmer A.G. III5
  • 19
    • 0030935462 scopus 로고    scopus 로고
    • Correlated bond rotations in interactions of arginine residues with ligand carboxylate groups in protein ligand complexes
    • Nieto PM, Birdsall B, Morgan WD, Frenkiel TA, Gargaro AR, Feeney J Correlated bond rotations in interactions of arginine residues with ligand carboxylate groups in protein ligand complexes. FEBS Lett. 405:1997;16-20.
    • (1997) FEBS Lett , vol.405 , pp. 16-20
    • Nieto, P.M.1    Birdsall, B.2    Morgan, W.D.3    Frenkiel, T.A.4    Gargaro, A.R.5    Feeney, J.6
  • 20
    • 0031565727 scopus 로고    scopus 로고
    • The NMR solution conformation of unligated human cyclophilin A
    • Ottiger M, Zerbe O, Güntert P, Wüthrich K The NMR solution conformation of unligated human cyclophilin A. J Mol Biol. 272:1997;64-81.
    • (1997) J Mol Biol , vol.272 , pp. 64-81
    • Ottiger, M.1    Zerbe, O.2    Güntert, P.3    Wüthrich, K.4
  • 21
    • 0031036243 scopus 로고    scopus 로고
    • Discrete backbone disorder in the nuclear magnetic resonance structure of apo intestinal fatty acid-binding protein: Implications for the mechanism of ligand entry
    • ••].
    • ••].
    • (1997) Biochemistry , vol.36 , pp. 1450-1460
    • Hodson, M.E.1    Cistola, D.P.2
  • 22
    • 0031043596 scopus 로고    scopus 로고
    • 1H exchange
    • •], provides a detailed analysis of the mobility of a discrete region in intestinal fatty-acid binding protein and the way in which this changes on fatty acid binding. It is proposed that this mobility is required for access of the fatty acid to its binding site.
    • •], provides a detailed analysis of the mobility of a discrete region in intestinal fatty-acid binding protein and the way in which this changes on fatty acid binding. It is proposed that this mobility is required for access of the fatty acid to its binding site.
    • (1997) Biochemistry , vol.36 , pp. 2278-2290
    • Hodson, M.E.1    Cistola, D.P.2
  • 24
    • 0031566963 scopus 로고    scopus 로고
    • 15N relaxation with monomer/dimer equilibration
    • 15N relaxation with monomer/dimer equilibration. J Mol Biol. 266:1997;173-194.
    • (1997) J Mol Biol , vol.266 , pp. 173-194
    • Fushman, D.1    Dahill, S.2    Cowburn, D.3
  • 26
    • 0031001259 scopus 로고    scopus 로고
    • Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 phosphotyrosine binding domain upon binding to an interleukin 4 receptor phosphopeptide
    • 15N relaxation studies show that many residues involved in peptide binding are motionally restricted in the free protein; others become more restricted on peptide binding - including some residues that do not contact the ligand directly.
    • 15N relaxation studies show that many residues involved in peptide binding are motionally restricted in the free protein; others become more restricted on peptide binding - including some residues that do not contact the ligand directly.
    • (1997) Biochemistry , vol.36 , pp. 4118-4124
    • Olejniczak, E.T.1    Zhou, M.-M.2    Fesik, S.W.3
  • 27
    • 0031564611 scopus 로고    scopus 로고
    • 13C chemical shifts
    • The NMR structure of this peptide-SH3 domain complex shows that the peptide residues in the first and second subsites are well-ordered, but a range of evidence is presented for mobility in the third subsite. The possibility of fluctuating hydrogen bonding interactions is discussed in which a donor on the peptide or protein can interact with alternative acceptors on the other partner.
    • 13C chemical shifts. J Mol Biol. 267:1997;933-952. The NMR structure of this peptide-SH3 domain complex shows that the peptide residues in the first and second subsites are well-ordered, but a range of evidence is presented for mobility in the third subsite. The possibility of fluctuating hydrogen bonding interactions is discussed in which a donor on the peptide or protein can interact with alternative acceptors on the other partner.
    • (1997) J Mol Biol , vol.267 , pp. 933-952
    • Wittekind, M.1    Mapelli Lee, V.2    Goldfarb, V.3    Friedrichs, M.S.4    Meyers, C.A.5    Mueller, L.6
  • 28
    • 0031910945 scopus 로고    scopus 로고
    • Correlation between binding and dynamics at SH2 domain interfaces
    • 2H relaxation measurements on methyl groups of two SH2 domains were used to probe changes in their dynamics on binding peptides. Both increases and decreases in mobility were observed, and the two domains showed different patterns of behaviour. The paper contains a valuable discussion of the relationships between dynamics, binding thermodynamics and specificity.
    • 2H relaxation measurements on methyl groups of two SH2 domains were used to probe changes in their dynamics on binding peptides. Both increases and decreases in mobility were observed, and the two domains showed different patterns of behaviour. The paper contains a valuable discussion of the relationships between dynamics, binding thermodynamics and specificity.
    • (1998) Nat Struct Biol , vol.5 , pp. 156-163
    • Kay, L.E.1    Muhandiram, D.R.2    Wolf, G.3    Shoelson, S.E.4    Forman-Kay, J.D.5
  • 29
    • 0030299991 scopus 로고    scopus 로고
    • 15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase: Backbone dynamics and entropy changes of an enzyme upon inhibitor binding
    • 15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase: backbone dynamics and entropy changes of an enzyme upon inhibitor binding. Biochemistry. 35:1996;16036-16047.
    • (1996) Biochemistry , vol.35 , pp. 16036-16047
    • Stivers, J.T.1    Abeygunawardana, C.2    Mildvan, A.S.3    Whitman, C.P.4
  • 31
    • 0030601792 scopus 로고    scopus 로고
    • Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: Application to protein folding
    • Yang D, Kay LE Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding. J Mol Biol. 263:1996;369-382.
    • (1996) J Mol Biol , vol.263 , pp. 369-382
    • Yang, D.1    Kay, L.E.2
  • 32
    • 0025308955 scopus 로고
    • NMR studies of interactions of ligands with dihydrofolate reductase
    • Feeney J NMR studies of interactions of ligands with dihydrofolate reductase. Biochem Pharmacol. 40:1990;141-152.
    • (1990) Biochem Pharmacol , vol.40 , pp. 141-152
    • Feeney, J.1
  • 33
    • 0013648071 scopus 로고    scopus 로고
    • NMR studies of ligand binding to dihydrofolate reductase and their applications in drug design
    • D. Craik. New York: CRC Press
    • Feeney J NMR studies of ligand binding to dihydrofolate reductase and their applications in drug design. Craik D NMR and Drug Design. 1996;CRC Press, New York.
    • (1996) NMR and Drug Design
    • Feeney, J.1
  • 34
    • 0031054786 scopus 로고    scopus 로고
    • The influence of aspartate 26 on the tautomeric forms of folate bound to Lactobacillus casei dihydrofolate reductase
    • 13C-Asp]-labelled enzyme was used to study the ionisation state of the active-site aspartic acid.
    • 13C-Asp]-labelled enzyme was used to study the ionisation state of the active-site aspartic acid.
    • (1997) FEBS Lett , vol.402 , pp. 157-161
    • Birdsall, B.1    Casarotto, M.G.2    Cheung, A.H.T.3    Basran, J.4    Roberts, G.C.K.5    Feeney, J.6
  • 35
    • 0001201663 scopus 로고    scopus 로고
    • Fast-HMQC using Ernst angle pulses: An efficient tool for screening of ligand binding to target proteins
    • Ross A, Slazmann M, Senn H Fast-HMQC using Ernst angle pulses: an efficient tool for screening of ligand binding to target proteins. J Biomol NMR. 10:1997;389-396.
    • (1997) J Biomol NMR , vol.10 , pp. 389-396
    • Ross, A.1    Slazmann, M.2    Senn, H.3
  • 37
    • 0032515399 scopus 로고    scopus 로고
    • Exploring the leucine-proline binding pocket of the Src SH3 domain using structure-based, split-pool synthesis and affinity-based selection
    • Morken JP, Kapoor TM, Feng S, Shirai F, Schreiber SL Exploring the leucine-proline binding pocket of the Src SH3 domain using structure-based, split-pool synthesis and affinity-based selection. J Am Chem Soc. 120:1998;30-36.
    • (1998) J Am Chem Soc , vol.120 , pp. 30-36
    • Morken, J.P.1    Kapoor, T.M.2    Feng, S.3    Shirai, F.4    Schreiber, S.L.5
  • 39
    • 0032478693 scopus 로고    scopus 로고
    • Identification of binding sites for beperidil and trifluoperazine on cardiac troponin C
    • Kleerekoper Q, Liu W, Choi D, Putkey JA Identification of binding sites for beperidil and trifluoperazine on cardiac troponin C. J Biol Chem. 273:1998;8153-8160.
    • (1998) J Biol Chem , vol.273 , pp. 8153-8160
    • Kleerekoper, Q.1    Liu, W.2    Choi, D.3    Putkey, J.A.4
  • 40
    • 0025252231 scopus 로고
    • 1H NMR spectroscopy - combined use with isotope labeling for studies of macromolecular conformation and intermolecular interactions
    • 1H NMR spectroscopy - combined use with isotope labeling for studies of macromolecular conformation and intermolecular interactions. Q Rev Biophys. 23:1990;39-96.
    • (1990) Q Rev Biophys , vol.23 , pp. 39-96
    • Otting, G.1    Wüthrich, K.2
  • 41
    • 0030808350 scopus 로고    scopus 로고
    • Methods for the measurement of intermolecular NOEs by multinuclear NMR spectroscopy: Application to a bacteriophage I N-peptide/box B RNA complex
    • Zwahlen C, Legault P, Vincent SJF, Greenblatt J, Konrat R, Kay LE Methods for the measurement of intermolecular NOEs by multinuclear NMR spectroscopy: application to a bacteriophage I N-peptide/box B RNA complex. J Am Chem Soc. 119:1997;6711-6721.
    • (1997) J Am Chem Soc , vol.119 , pp. 6711-6721
    • Zwahlen, C.1    Legault, P.2    Vincent, S.J.F.3    Greenblatt, J.4    Konrat, R.5    Kay, L.E.6
  • 43
    • 0029123503 scopus 로고
    • Solution structure of a brodimoprim analog in its complex with Lactobacillus casei dihydrofolate reductase
    • Morgan WD, Birdsall B, Polshakov VI, Sali D, Kompis I, Feeney J Solution structure of a brodimoprim analog in its complex with Lactobacillus casei dihydrofolate reductase. Biochemistry. 34:1995;11690-11702.
    • (1995) Biochemistry , vol.34 , pp. 11690-11702
    • Morgan, W.D.1    Birdsall, B.2    Polshakov, V.I.3    Sali, D.4    Kompis, I.5    Feeney, J.6
  • 44
    • 0030936561 scopus 로고    scopus 로고
    • NMR solution structure of the antitumor compound PT523 and NADPH in the ternary complex with human dihydrofolate reductase
    • Johnson J, Meiering EM, Wright JE, Pardo J, Rosowsky A, Wagner G NMR solution structure of the antitumor compound PT523 and NADPH in the ternary complex with human dihydrofolate reductase. Biochemistry. 36:1997;4399-4411.
    • (1997) Biochemistry , vol.36 , pp. 4399-4411
    • Johnson, J.1    Meiering, E.M.2    Wright, J.E.3    Pardo, J.4    Rosowsky, A.5    Wagner, G.6
  • 45
    • 0031450585 scopus 로고    scopus 로고
    • Bioactive conformation of a potent stromelysin inhibitor determined by X-nucleus filtered and multidimensional NMR spectroscopy
    • Gonnella NC, Li YC, Zhang XL, Paris CG Bioactive conformation of a potent stromelysin inhibitor determined by X-nucleus filtered and multidimensional NMR spectroscopy. Bioorg Med Chem. 5:1997;2193-2201.
    • (1997) Bioorg Med Chem , vol.5 , pp. 2193-2201
    • Gonnella, N.C.1    Li, Y.C.2    Zhang, X.L.3    Paris, C.G.4
  • 46
    • 0029715474 scopus 로고    scopus 로고
    • Validation of the use of intermolecular NOE constraints for obtaining docked structures of protein-ligand complexes
    • Gradwell MJ, Feeney J Validation of the use of intermolecular NOE constraints for obtaining docked structures of protein-ligand complexes. J Biomol NMR. 7:1996;48-58.
    • (1996) J Biomol NMR , vol.7 , pp. 48-58
    • Gradwell, M.J.1    Feeney, J.2
  • 48
    • 0030963409 scopus 로고    scopus 로고
    • 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine as a substrate of cytochrome P450 2D6: Allosteric effects of NADPH-cytochrome P450 reductase
    • Paramagnetic relaxation experiments (see [47]) are used to measure distances from the haem iron to protons of the substrate bound to P450 2D6. These experiments show that, in the presence of P450 reductase but not in its absence, the substrate can bind in two different orientations, which correspond to the two products formed. This illustrates the usefulness of the paramagnetic relaxation approach in studying the specificity of P450s.
    • Modi S, Gilham DE, Sutcliffe MJ, Lian L-Y, Primrose WU, Wolf CR, Roberts GCK 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine as a substrate of cytochrome P450 2D6: allosteric effects of NADPH-cytochrome P450 reductase. Biochemistry. 36:1997;4461-4470. Paramagnetic relaxation experiments (see [47]) are used to measure distances from the haem iron to protons of the substrate bound to P450 2D6. These experiments show that, in the presence of P450 reductase but not in its absence, the substrate can bind in two different orientations, which correspond to the two products formed. This illustrates the usefulness of the paramagnetic relaxation approach in studying the specificity of P450s.
    • (1997) Biochemistry , vol.36 , pp. 4461-4470
    • Modi, S.1    Gilham, D.E.2    Sutcliffe, M.J.3    Lian, L.-Y.4    Primrose, W.U.5    Wolf, C.R.6    Roberts, G.C.K.7
  • 49
    • 0029876059 scopus 로고    scopus 로고
    • The catalytic mechanism of cytochrome P450 BM3 involves a 6 Å movement of the bound substrate on reduction
    • Modi S, Sutcliffe MJ, Primrose WU, Lian L-Y, Roberts GCK The catalytic mechanism of cytochrome P450 BM3 involves a 6 Å movement of the bound substrate on reduction. Nat Struct Biol. 3:1996;414-417.
    • (1996) Nat Struct Biol , vol.3 , pp. 414-417
    • Modi, S.1    Sutcliffe, M.J.2    Primrose, W.U.3    Lian, L.-Y.4    Roberts, G.C.K.5
  • 50
    • 0031033653 scopus 로고    scopus 로고
    • A single-residue mutation in cytochrome P450 changes the substrate orientation in a catalytic intermediate and the regiospecificity of hydroxylation
    • Oliver CF, Modi S, Sutcliffe MJ, Primrose WU, Lian L-Y, Roberts GCK A single-residue mutation in cytochrome P450 changes the substrate orientation in a catalytic intermediate and the regiospecificity of hydroxylation. Biochemistry. 36:1997;1567-1572.
    • (1997) Biochemistry , vol.36 , pp. 1567-1572
    • Oliver, C.F.1    Modi, S.2    Sutcliffe, M.J.3    Primrose, W.U.4    Lian, L.-Y.5    Roberts, G.C.K.6
  • 51
    • 0030687597 scopus 로고    scopus 로고
    • The substrate binding site of human liver cytochrome P450 2C9: An NMR study
    • Paramagnetic relaxation experiments are used to position several substrates relative to the haem iron of P450 2C9, and to identify features of the active site (e.g. the location of a putative positive charge) from the superposition of the substrates.
    • Poli-Scaife S, Attias R, Dansette PM, Mansuy D The substrate binding site of human liver cytochrome P450 2C9: an NMR study. Biochemistry. 36:1997;12672-12682. Paramagnetic relaxation experiments are used to position several substrates relative to the haem iron of P450 2C9, and to identify features of the active site (e.g. the location of a putative positive charge) from the superposition of the substrates.
    • (1997) Biochemistry , vol.36 , pp. 12672-12682
    • Poli-Scaife, S.1    Attias, R.2    Dansette, P.M.3    Mansuy, D.4
  • 52
    • 0002860359 scopus 로고
    • The use of transferred nuclear Overhauser effects in the study of the conformation of small molecules bound to proteins
    • Albrand JP, Birdsall B, Feeney J, Roberts CK, Burgen ASV The use of transferred nuclear Overhauser effects in the study of the conformation of small molecules bound to proteins. Int J Biol Macromol. 1:1979;37-41.
    • (1979) Int J Biol Macromol , vol.1 , pp. 37-41
    • Albrand, J.P.1    Birdsall, B.2    Feeney, J.3    Roberts, C.K.4    Burgen, A.S.V.5
  • 53
    • 0000393431 scopus 로고
    • Theory and application of the transferred nuclear Overhauser effect to the study of the conformations of small ligands bound to proteins
    • Clore GM, Gronenborn AM Theory and application of the transferred nuclear Overhauser effect to the study of the conformations of small ligands bound to proteins. J Magn Reson. 48:1982;402-417.
    • (1982) J Magn Reson , vol.48 , pp. 402-417
    • Clore, G.M.1    Gronenborn, A.M.2
  • 54
    • 0027215829 scopus 로고
    • The two-dimensional transferred nuclear Overhauser effect - theory and practice
    • Campbell AP, Sykes BD The two-dimensional transferred nuclear Overhauser effect - theory and practice. Annu Rev Biophys Biomol Struct. 22:1993;99-122.
    • (1993) Annu Rev Biophys Biomol Struct , vol.22 , pp. 99-122
    • Campbell, A.P.1    Sykes, B.D.2
  • 55
    • 0028728698 scopus 로고
    • Recent advances in transferred NOE methods
    • Ni F Recent advances in transferred NOE methods. Prog NMR Spectrosc. 26:1994;517-605.
    • (1994) Prog NMR Spectrosc , vol.26 , pp. 517-605
    • Ni, F.1
  • 56
    • 0031837381 scopus 로고    scopus 로고
    • Transferred nuclear Overhauser effect study of macrolide-ribosome interactions: Correlation between antibiotic activities and bound conformations
    • Bertho G, Gharbi-Benarous J, Delaforge M, Girault JP Transferred nuclear Overhauser effect study of macrolide-ribosome interactions: correlation between antibiotic activities and bound conformations. Bioorg Med Chem. 6:1998;209-221.
    • (1998) Bioorg Med Chem , vol.6 , pp. 209-221
    • Bertho, G.1    Gharbi-Benarous, J.2    Delaforge, M.3    Girault, J.P.4
  • 57
    • 0029243119 scopus 로고
    • Identification of protein-mediated indirect NOE effects in a disaccharide-Fab′ complex by transferred ROESY
    • Arepalli SR, Glaudemans CPJ, Daves GD, Kovac P, Bax A Identification of protein-mediated indirect NOE effects in a disaccharide-Fab′ complex by transferred ROESY. J Magn Reson B. 106:1995;195-198.
    • (1995) J Magn Reson B , vol.106 , pp. 195-198
    • Arepalli, S.R.1    Glaudemans, C.P.J.2    Daves, G.D.3    Kovac, P.4    Bax, A.5
  • 58
    • 0030568979 scopus 로고    scopus 로고
    • The conformation of coenzyme A bound to chloramphenicol acetyltransferase determined by transferred NOE experiments
    • Barsukov IL, Lian L-Y, Ellis J, Sze K-H, Shaw WV, Roberts GCK The conformation of coenzyme A bound to chloramphenicol acetyltransferase determined by transferred NOE experiments. J Mol Biol. 262:1996;543-558.
    • (1996) J Mol Biol , vol.262 , pp. 543-558
    • Barsukov, I.L.1    Lian, L.-Y.2    Ellis, J.3    Sze, K.-H.4    Shaw, W.V.5    Roberts, G.C.K.6
  • 59
    • 0030726350 scopus 로고    scopus 로고
    • Conformation of the trypanocidal pharmaceutical in its free and bound forms: Transferred nuclear Overhauser studies
    • Polenova T, Iwashita T, Palmer AG III, McDermott AE Conformation of the trypanocidal pharmaceutical in its free and bound forms: transferred nuclear Overhauser studies. Biochemistry. 36:1997;14202-14217.
    • (1997) Biochemistry , vol.36 , pp. 14202-14217
    • Polenova, T.1    Iwashita, T.2    Palmer A.G. III3    McDermott, A.E.4
  • 60
    • 0000239022 scopus 로고
    • Elimination of multiple-step spin diffusion effects in two-dimensional NOE spectroscopy of nucleic acids
    • Massefski W, Redfield AG Elimination of multiple-step spin diffusion effects in two-dimensional NOE spectroscopy of nucleic acids. J Magn Reson. 78:1988;150-155.
    • (1988) J Magn Reson , vol.78 , pp. 150-155
    • Massefski, W.1    Redfield, A.G.2
  • 61
    • 21844493556 scopus 로고
    • Magnetization exchange network editing - mathematical principles and experimental demonstration
    • Zolnai Z, Juranic N, Markley JL, Macura S Magnetization exchange network editing - mathematical principles and experimental demonstration. Chem Phys. 200:1995;161-179.
    • (1995) Chem Phys , vol.200 , pp. 161-179
    • Zolnai, Z.1    Juranic, N.2    Markley, J.L.3    Macura, S.4
  • 62
    • 0031114880 scopus 로고    scopus 로고
    • Identification of spin diffusion pathways in proteins by isotope-assisted NMR cross-relaxation network editing
    • Juranic N, Zolnai Z, Macura S Identification of spin diffusion pathways in proteins by isotope-assisted NMR cross-relaxation network editing. J Biomol NMR. 9:1997;317-322.
    • (1997) J Biomol NMR , vol.9 , pp. 317-322
    • Juranic, N.1    Zolnai, Z.2    Macura, S.3
  • 63
    • 0030894827 scopus 로고    scopus 로고
    • + bound to lactate dehydrogenase determined by nuclear magnetic resonance with suppression of spin diffusion
    • + was similar to that seen in the crystal, but that about the nicotinamide glycosidic bond was not, and the coexistence of two conformations about this bond in the complex is suggested
    • + was similar to that seen in the crystal, but that about the nicotinamide glycosidic bond was not, and the coexistence of two conformations about this bond in the complex is suggested.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4383-4388
    • Vincent, S.J.F.1    Zwahlen, C.2    Post, C.B.3    Burgner, J.W.4    Bodenhausen, G.5
  • 64
    • 0031017444 scopus 로고    scopus 로고
    • Biologically important conformations of aminoglycoside antibiotics bound to an aminoglycoside 3′-phosphotransferase as determined by transferred nuclear Overhauser effect spectroscopy
    • Cox JR, Serpersu EH Biologically important conformations of aminoglycoside antibiotics bound to an aminoglycoside 3′-phosphotransferase as determined by transferred nuclear Overhauser effect spectroscopy. Biochemistry. 36:1997;2353-2359.
    • (1997) Biochemistry , vol.36 , pp. 2353-2359
    • Cox, J.R.1    Serpersu, E.H.2
  • 65
    • 0032478261 scopus 로고    scopus 로고
    • Solution structure of glutathione bound to human glutathione transferase P1-1: Comparison of NMR measurements with the crystal structure
    • Transferred NOE experiments lead to a conformation of bound glutathione that has a similar backbone conformation but sidechain conformations that differ from those seen in the crystal. The origins of this difference are discussed in the light of docking calculations and kinetic experiments; it is concluded that the NMR structure may correspond to that of a 'pre-complex' (see also [58])
    • Nicotra M, Paci M, Sette M, Oakley AJ, Parker MW, Lo Bello M, Caccuri AM, Federici G, Ricci G Solution structure of glutathione bound to human glutathione transferase P1-1: comparison of NMR measurements with the crystal structure. Biochemistry. 37:1998;3020-3027. Transferred NOE experiments lead to a conformation of bound glutathione that has a similar backbone conformation but sidechain conformations that differ from those seen in the crystal. The origins of this difference are discussed in the light of docking calculations and kinetic experiments; it is concluded that the NMR structure may correspond to that of a 'pre-complex' (see also [58]).
    • (1998) Biochemistry , vol.37 , pp. 3020-3027
    • Nicotra, M.1    Paci, M.2    Sette, M.3    Oakley, A.J.4    Parker, M.W.5    Lo Bello, M.6    Caccuri, A.M.7    Federici, G.8    Ricci, G.9
  • 66
    • 0032542581 scopus 로고    scopus 로고
    • Escherichia coli β-galactosidase recognizes a high-energy conformation of C-lactose, a non-hydrolyzable substrate analogue. NMR and modelling studies of the molecular complex
    • Transferred NOE experiments indicate that C-lactose (in which the glycosidic oxygen of lactose is replaced by a methylene group) bound to β-galactosidase adopts a conformation which is only slightly populated (~5%) in the free ligand.
    • Espinosa JF, Montero E, Vian A, García JL, Dietrich H, Schmidt RR, Martín-Lomas M, Imberty A, Cañada FJ, Jiménez-Barbero J Escherichia coli β-galactosidase recognizes a high-energy conformation of C-lactose, a non-hydrolyzable substrate analogue. NMR and modelling studies of the molecular complex. J Am Chem Soc. 120:1998;1309-1318. Transferred NOE experiments indicate that C-lactose (in which the glycosidic oxygen of lactose is replaced by a methylene group) bound to β-galactosidase adopts a conformation which is only slightly populated (~5%) in the free ligand.
    • (1998) J Am Chem Soc , vol.120 , pp. 1309-1318
    • Espinosa, J.F.1    Montero, E.2    Vian, A.3    García, J.L.4    Dietrich, H.5    Schmidt, R.R.6    Martín-Lomas, M.7    Imberty, A.8    Cañada, F.J.9    Jiménez-Barbero, J.10
  • 68
    • 0030899123 scopus 로고    scopus 로고
    • x tetrasaccharide free in solution and bound to E-, P-, and L-selectin
    • x tetrasaccharide, the sialyl residue is attached via a flexible glycosidic linkage to a rigid branched trisaccharide. A careful quantitative analysis of transferred NOE experiments shows that different conformers of the tetrasaccharide are recognised by E- and P-selectin on the one hand and L-selectin on the other.
    • x tetrasaccharide, the sialyl residue is attached via a flexible glycosidic linkage to a rigid branched trisaccharide. A careful quantitative analysis of transferred NOE experiments shows that different conformers of the tetrasaccharide are recognised by E- and P-selectin on the one hand and L-selectin on the other.
    • (1997) J Am Chem Soc , vol.119 , pp. 1727-1736
    • Poppe, L.1    Brown, G.S.2    Philo, J.S.3    Nikrad, P.V.4    Shah, B.H.5
  • 70
    • 0032519515 scopus 로고    scopus 로고
    • Mapping the active site of factor Xa by selective inhibitors: And NMR and MD study
    • Two peptide inhibitors of factor Xa, obtained by library screening, were studied by transferred NOE experiments. Structures were calculated both for the peptides in isolation and in the binding site (see also [58]), systematically exploring possible orientations in the site. The model of the complex obtained, suggesting that the inhibitors bind differently from the substrate, made it possible to explain the specificity of the inhibitors.
    • Fraternali F, Do Q-T, Doan B-T, Atkinson RA, Palmas P, Sklenar V, Safar P, Wildgoose P, Strop P, Saudek V Mapping the active site of factor Xa by selective inhibitors: and NMR and MD study. Proteins Struct Func Genet. 30:1998;264-274. Two peptide inhibitors of factor Xa, obtained by library screening, were studied by transferred NOE experiments. Structures were calculated both for the peptides in isolation and in the binding site (see also [58]), systematically exploring possible orientations in the site. The model of the complex obtained, suggesting that the inhibitors bind differently from the substrate, made it possible to explain the specificity of the inhibitors.
    • (1998) Proteins Struct Func Genet , vol.30 , pp. 264-274
    • Fraternali, F.1    Do, Q.-T.2    Doan, B.-T.3    Atkinson, R.A.4    Palmas, P.5    Sklenar, V.6    Safar, P.7    Wildgoose, P.8    Strop, P.9    Saudek, V.10
  • 71
    • 0032548447 scopus 로고    scopus 로고
    • Insights into tyrosine phosphorylation control of protein-protein association from the NMR structure of a band 3 peptide inhibitor bound to glyceraldehyde-3-phosphate dehydrogenase
    • Eisenmesser EZ, Post CB Insights into tyrosine phosphorylation control of protein-protein association from the NMR structure of a band 3 peptide inhibitor bound to glyceraldehyde-3-phosphate dehydrogenase. Biochemistry. 37:1998;867-877.
    • (1998) Biochemistry , vol.37 , pp. 867-877
    • Eisenmesser, E.Z.1    Post, C.B.2
  • 72
    • 0032575343 scopus 로고    scopus 로고
    • NMR studies on the conformation of the CD4 36-59 peptide bound to HIV gp120
    • Transferred NOE experiments, including identification of spin diffusion effects, led to a well-defined backbone conformation for residues 42-49 of the peptide corresponding to CD4 residues 36-59 when bound to HIV-1 gp120. The calculated conformation differed from that seen in either of two crystal structures of CD4, suggesting a change in conformation on binding.
    • Gizachew D, Moffett DB, Busse SC, Westler WM, Dratz EA, Teintze M NMR studies on the conformation of the CD4 36-59 peptide bound to HIV gp120. Biochemistry. 37:1998;10616-10625. Transferred NOE experiments, including identification of spin diffusion effects, led to a well-defined backbone conformation for residues 42-49 of the peptide corresponding to CD4 residues 36-59 when bound to HIV-1 gp120. The calculated conformation differed from that seen in either of two crystal structures of CD4, suggesting a change in conformation on binding.
    • (1998) Biochemistry , vol.37 , pp. 10616-10625
    • Gizachew, D.1    Moffett, D.B.2    Busse, S.C.3    Westler, W.M.4    Dratz, E.A.5    Teintze, M.6
  • 73
    • 0031558779 scopus 로고    scopus 로고
    • Structure of the fifth EGF-like domain of thrombomodulin: An EGF-like domain with a novel disulfide-bonding pattern
    • •] show the value of transferred NOE experiments in giving access to the peptide conformation in the bound state, as a model for the design of peptidomimetic drugs.
    • •] show the value of transferred NOE experiments in giving access to the peptide conformation in the bound state, as a model for the design of peptidomimetic drugs.
    • (1997) J Mol Biol , vol.273 , pp. 913-926
    • Benitez, B.A.S.1    Hunter, M.J.2    Meininger, D.P.3    Komives, E.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.