메뉴 건너뛰기




Volumn 322, Issue 2, 2002, Pages 425-440

Detection and characterization of xenon-binding sites in proteins by 129Xe NMR spectroscopy

Author keywords

Hydrophobic cavities; Ligand protein interactions; Multiple isomorphous replacement; Protein conformation assay; Xenon binding

Indexed keywords

MALTOSE BINDING PROTEIN; PROTEIN; UNCLASSIFIED DRUG; XENON; XENON 129;

EID: 0036385795     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00739-8     Document Type: Article
Times cited : (105)

References (55)
  • 1
    • 0013842370 scopus 로고
    • Binding of xenon to sperm whale myoglobin
    • Schoenborn, B. C., Watson, H. C., & Kendrew, J. C. (1965). Binding of xenon to sperm whale myoglobin. Nature, 207, 28-30.
    • (1965) Nature , vol.207 , pp. 28-30
    • Schoenborn, B.C.1    Watson, H.C.2    Kendrew, J.C.3
  • 2
    • 0031180380 scopus 로고    scopus 로고
    • Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics
    • Montet, Y., Amara, P., Volbeda, A., Vernede, X., Hatchikian, E. C., Field, M. J. et al. (1997). Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics. Nature Struct. Biol. 4, 523-526.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 523-526
    • Montet, Y.1    Amara, P.2    Volbeda, A.3    Vernede, X.4    Hatchikian, E.C.5    Field, M.J.6
  • 4
    • 0035957218 scopus 로고    scopus 로고
    • Xenon and halogenated alkanes track putative substrate binding cavities in the soluble methane monooxygenase hydroxylase
    • Whittington, D. A., Rosenzweig, A. C., Frederick, C. A. & Lippard, S. J. (2001). Xenon and halogenated alkanes track putative substrate binding cavities in the soluble methane monooxygenase hydroxylase. Biochemistry, 40, 3476-3482.
    • (2001) Biochemistry , vol.40 , pp. 3476-3482
    • Whittington, D.A.1    Rosenzweig, A.C.2    Frederick, C.A.3    Lippard, S.J.4
  • 6
    • 0034730366 scopus 로고    scopus 로고
    • Modeling protein-small molecule interactions: Structure and thermodynamics of noble gases binding in a cavity in mutant phage T4 lysozyme L99A
    • Mann, G. & Hermans, J. (2000). Modeling protein-small molecule interactions: structure and thermodynamics of noble gases binding in a cavity in mutant phage T4 lysozyme L99A. J. Mol. Biol. 302, 979-989.
    • (2000) J. Mol. Biol. , vol.302 , pp. 979-989
    • Mann, G.1    Hermans, J.2
  • 7
    • 0034730423 scopus 로고    scopus 로고
    • Size versus polarizability in protein-ligand interactions: Binding of noble gases within engineered cavities in phage T4 lysozyme
    • Quillin, M. L., Breyer, W. A., Griswold, I. J. & Matthews, B. W. (2000). Size versus polarizability in protein-ligand interactions: binding of noble gases within engineered cavities in phage T4 lysozyme. J. Mol. Biol. 302, 955-977.
    • (2000) J. Mol. Biol. , vol.302 , pp. 955-977
    • Quillin, M.L.1    Breyer, W.A.2    Griswold, I.J.3    Matthews, B.W.4
  • 8
    • 0034809352 scopus 로고    scopus 로고
    • Electron spin catalysis by xenon in an enzyme
    • Anderson, M., Xu, Y. & Grissom, C. B. (2001). Electron spin catalysis by xenon in an enzyme. J. Am. Chem. Soc. 123, 6720-6721.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 6720-6721
    • Anderson, M.1    Xu, Y.2    Grissom, C.B.3
  • 9
    • 0028736397 scopus 로고
    • On the preparation and X-ray data collection of isomorphous derivatives
    • Schiltz, M., Prangé, T. & Fourme, R. (1994). On the preparation and X-ray data collection of isomorphous derivatives. J. Appl. Crystallog. 27, 950-960.
    • (1994) J. Appl. Crystallog. , vol.27 , pp. 950-960
    • Schiltz, M.1    Prangé, T.2    Fourme, R.3
  • 11
    • 0031903288 scopus 로고    scopus 로고
    • MAD phasing grows up
    • Ogata, C. M. (1998). MAD phasing grows up. Nature Struct. Biol. 5, 638-640.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 638-640
    • Ogata, C.M.1
  • 12
    • 0032514874 scopus 로고    scopus 로고
    • A structural explanation for the recognition of tyrosine-based endocytotic signals
    • Owen, D. J. & Evans, P. R. (1998). A structural explanation for the recognition of tyrosine-based endocytotic signals. Science, 282, 1327-1332.
    • (1998) Science , vol.282 , pp. 1327-1332
    • Owen, D.J.1    Evans, P.R.2
  • 13
    • 0033536633 scopus 로고    scopus 로고
    • Crystal structure of invasin: A bacterial integrin-binding protein
    • Hamburger, Z. A., Brown, M. S., Isberg, R. R. & Bjorkman, P. J. (1999). Crystal structure of invasin: a bacterial integrin-binding protein. Science, 286, 291-295.
    • (1999) Science , vol.286 , pp. 291-295
    • Hamburger, Z.A.1    Brown, M.S.2    Isberg, R.R.3    Bjorkman, P.J.4
  • 16
    • 0020285568 scopus 로고
    • Nuclear magnetic resonance studies of xenon-129 with myoglobin and hemoglobin
    • Tilton, R. F., Jr & Kuntz, I. D., Jr (1982). Nuclear magnetic resonance studies of xenon-129 with myoglobin and hemoglobin. Biochemistry, 21, 6850-6857.
    • (1982) Biochemistry , vol.21 , pp. 6850-6857
    • Tilton R.F., Jr.1    Kuntz I.D., Jr.2
  • 17
    • 0028093560 scopus 로고
    • Evidence of xenon transport through the gramicidin channel: A 129-Xe NMR study
    • McKim, S. & Hinton, J. F. (1994). Evidence of xenon transport through the gramicidin channel: a 129-Xe NMR study. Biochim. Biophys. Acta, 1193, 186-198.
    • (1994) Biochim. Biophys. Acta , vol.1193 , pp. 186-198
    • McKim, S.1    Hinton, J.F.2
  • 19
    • 0031480383 scopus 로고    scopus 로고
    • Spin-exchange optical pumping of noble-gas nuclei
    • Walker, T. G. & Happer, W. (1997). Spin-exchange optical pumping of noble-gas nuclei. Rev. Mod. Phys. 69, 629-642.
    • (1997) Rev. Mod. Phys. , vol.69 , pp. 629-642
    • Walker, T.G.1    Happer, W.2
  • 20
    • 0033552298 scopus 로고    scopus 로고
    • Exploring surfaces and cavities in lipoxygenase and other proteins by hyperpolarized xenon-129 NMR
    • Bowers, C. R., Storhaug, V., Webster, C. E., Bharatam, J., Cottone, A., Gianna, R. et al. (1999). Exploring surfaces and cavities in lipoxygenase and other proteins by hyperpolarized xenon-129 NMR. J. Am. Chem. Soc. 121, 9370-9377.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9370-9377
    • Bowers, C.R.1    Storhaug, V.2    Webster, C.E.3    Bharatam, J.4    Cottone, A.5    Gianna, R.6
  • 22
    • 0035088036 scopus 로고    scopus 로고
    • Magnetization transfer from laser-polarized xenon to protons in the hydrophobic cavity of the wheat nonspecific lipid tranfer protein
    • Landon, C., Berthault, P., Vovelle, F. & Desvaux, H. (2001). Magnetization transfer from laser-polarized xenon to protons in the hydrophobic cavity of the wheat nonspecific lipid tranfer protein. Protein Sci. 10, 762-770.
    • (2001) Protein Sci. , vol.10 , pp. 762-770
    • Landon, C.1    Berthault, P.2    Vovelle, F.3    Desvaux, H.4
  • 23
    • 0000813313 scopus 로고    scopus 로고
    • Enhancement of solution NMR and MRI with laser-polarized xenon
    • Navon, G., Song, Y. Q., Room, T., Appelt, S., Taylor, R. E. & Pines, A. (1996). Enhancement of solution NMR and MRI with laser-polarized xenon. Science, 271, 1848-1851.
    • (1996) Science , vol.271 , pp. 1848-1851
    • Navon, G.1    Song, Y.Q.2    Room, T.3    Appelt, S.4    Taylor, R.E.5    Pines, A.6
  • 26
    • 0034662996 scopus 로고    scopus 로고
    • Evidence of nonspecific surface interactions between laser-polarized xenon and myoglobin in solution
    • Rubin, S. M., Spence, M. M., Goodson, B. M., Wemmer, D. E. & Pines, A. (2000). Evidence of nonspecific surface interactions between laser-polarized xenon and myoglobin in solution. Proc. Natl Acad. Sci. USA, 97, 9472-9475.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9472-9475
    • Rubin, S.M.1    Spence, M.M.2    Goodson, B.M.3    Wemmer, D.E.4    Pines, A.5
  • 28
    • 0035743583 scopus 로고    scopus 로고
    • 129Xe chemical shifts in aqueous solution: Further development of xenon as a biomolecular probe
    • 129Xe chemical shifts in aqueous solution: further development of xenon as a biomolecular probe. J. Magn. Reson. 152, 79-86.
    • (2001) J. Magn. Reson. , vol.152 , pp. 79-86
    • Rubin, S.M.1    Spence, M.M.2    Pines, A.3    Wemmer, D.E.4
  • 29
    • 0026567907 scopus 로고
    • Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect
    • Eriksson, A. E., Baase, W. A., Zhang, X.-J., Heinz, D. W., Blaber, M., Baldwin, E. P. & Matthews, B. W. (1992). Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. Science, 255, 178-183.
    • (1992) Science , vol.255 , pp. 178-183
    • Eriksson, A.E.1    Baase, W.A.2    Zhang, X.-J.3    Heinz, D.W.4    Blaber, M.5    Baldwin, E.P.6    Matthews, B.W.7
  • 30
    • 0026493924 scopus 로고
    • Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodexrin binding protein involved in active transport and chemotaxis
    • Sharff, A. J., Rodseth, L. E., Spurlino, J. C. & Quiocho, F. A. (1992). Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodexrin binding protein involved in active transport and chemotaxis. Biochemistry, 31, 10657-10663.
    • (1992) Biochemistry , vol.31 , pp. 10657-10663
    • Sharff, A.J.1    Rodseth, L.E.2    Spurlino, J.C.3    Quiocho, F.A.4
  • 31
    • 0030606256 scopus 로고    scopus 로고
    • Crystal structures and solution conformations of a dominant-negative mutant of Escherichia coli maltose-binding protein
    • Shilton, B. H., Shuman, H. A. & Mowbray, S. L. (1996). Crystal structures and solution conformations of a dominant-negative mutant of Escherichia coli maltose-binding protein. J. Mol. Biol. 2, 364-376.
    • (1996) J. Mol. Biol. , vol.2 , pp. 364-376
    • Shilton, B.H.1    Shuman, H.A.2    Mowbray, S.L.3
  • 33
    • 0025754301 scopus 로고
    • The 2.3 Å resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis
    • Spurlino, J. C., Lu, G.-Y. & Quiocho, F. A. (1991). The 2.3 Å resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J. Biol. Chem. 266, 5202-5219.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5202-5219
    • Spurlino, J.C.1    Lu, G.-Y.2    Quiocho, F.A.3
  • 34
    • 0001592066 scopus 로고    scopus 로고
    • A simple device for studying macromolecular crystals under moderate gas pressures (0.1-10 MPa)
    • Stowell, M. H. B., Soltis, S. M., Kisker, C., Peters, J. W., Schindelin, H., Rees, D. C. et al. (1996). A simple device for studying macromolecular crystals under moderate gas pressures (0.1-10 MPa). J. Appl. Crystallog. 29, 608-613.
    • (1996) J. Appl. Crystallog. , vol.29 , pp. 608-613
    • Stowell, M.H.B.1    Soltis, S.M.2    Kisker, C.3    Peters, J.W.4    Schindelin, H.5    Rees, D.C.6
  • 35
    • 0027364214 scopus 로고
    • Refined 1.8 Å structure reveals the mode of binding of β-cyclodextrin to the maltodextrin binding protein
    • Sharff, A. J., Rodseth, L. E. & Quiocho, F. A. (1993). Refined 1.8 Å structure reveals the mode of binding of β-cyclodextrin to the maltodextrin binding protein. Biochemistry, 32, 10553-10559.
    • (1993) Biochemistry , vol.32 , pp. 10553-10559
    • Sharff, A.J.1    Rodseth, L.E.2    Quiocho, F.A.3
  • 36
    • 0034912592 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for high molecular weight proteins: A study involving a complex of maltose binding protein and beta-cyclodextrin
    • Kay, L. E. (2001). Nuclear magnetic resonance methods for high molecular weight proteins: a study involving a complex of maltose binding protein and beta-cyclodextrin. Methods Enzymol. 339, 174-203.
    • (2001) Methods Enzymol. , vol.339 , pp. 174-203
    • Kay, L.E.1
  • 37
    • 0032544978 scopus 로고    scopus 로고
    • Solution NMR studies of a 42 kDa Escherichia coli maltose binding protein/β-cyclodextrin complex: Chemical shift assignments and analysis
    • Gardner, K. H., Zhang, X., Gehring, K. & Kay, L. E. (1998). Solution NMR studies of a 42 kDa Escherichia coli maltose binding protein/β-cyclodextrin complex: Chemical shift assignments and analysis. J. Am. Chem. Soc. 120, 11738-11748.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11738-11748
    • Gardner, K.H.1    Zhang, X.2    Gehring, K.3    Kay, L.E.4
  • 38
    • 0029067489 scopus 로고
    • Specificity of ligand binding in a buried nonpolar cavity of T4 lysozyme: Linkage of dynamics and structural plasticity
    • Morton, A. & Matthews, B. W. (1995). Specificity of ligand binding in a buried nonpolar cavity of T4 lysozyme: linkage of dynamics and structural plasticity. Biochemistry, 34, 8576-8588.
    • (1995) Biochemistry , vol.34 , pp. 8576-8588
    • Morton, A.1    Matthews, B.W.2
  • 39
    • 0034680315 scopus 로고    scopus 로고
    • Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR
    • Mulder, F. A. A., Hon, B., Muhandiram, D. J., Dahlquist, F. W. & Kay, L. E. (2000). Flexibility and ligand exchange in a buried cavity mutant of T4 lysozyme studied by multinuclear NMR. Biochemistry, 39, 12614-12622.
    • (2000) Biochemistry , vol.39 , pp. 12614-12622
    • Mulder, F.A.A.1    Hon, B.2    Muhandiram, D.J.3    Dahlquist, F.W.4    Kay, L.E.5
  • 40
    • 0021766921 scopus 로고
    • Cavities in proteins: Structure of a metmyoglobin-xenon complex solved to 1.9 Å
    • Tilton, R. F., Jr, Kuntz, I. D., Jr & Petsko, G. A. (1984). Cavities in proteins: structure of a metmyoglobin-xenon complex solved to 1.9 Å. Biochemistry, 23, 2849-2857.
    • (1984) Biochemistry , vol.23 , pp. 2849-2857
    • Tilton R.F., Jr.1    Kuntz I.D., Jr.2    Petsko, G.A.3
  • 41
    • 37049082163 scopus 로고
    • The nuclear magnetic resonance of Xe-129 trapped in clathrates and some other solids
    • Ripmeester, J. A., Ratcliffe, C. I. & Tse, J. S. (1988). The nuclear magnetic resonance of Xe-129 trapped in clathrates and some other solids. J. Chem. Soc., Faraday Trans. 84, 3731-3745.
    • (1988) J. Chem. Soc., Faraday Trans. , vol.84 , pp. 3731-3745
    • Ripmeester, J.A.1    Ratcliffe, C.I.2    Tse, J.S.3
  • 42
    • 0040214688 scopus 로고    scopus 로고
    • Nuclear magnetic resonance of physisorbed 129-Xe used as a probe to investigate porous solids
    • Bonardet, J., Fraissard, J., Gédéon, A. & Springuel-Huet, M. (1999). Nuclear magnetic resonance of physisorbed 129-Xe used as a probe to investigate porous solids. Catal. Rev.: Sci. Eng. 41, 115-225.
    • (1999) Catal. Rev.: Sci. Eng. , vol.41 , pp. 115-225
    • Bonardet, J.1    Fraissard, J.2    Gédéon, A.3    Springuel-Huet, M.4
  • 44
    • 0031571605 scopus 로고    scopus 로고
    • Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor
    • Quiocho, F. A., Spurlino, J. C. & Rodseth, L. E. (1997). Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor. Structure, 5, 997-1015.
    • (1997) Structure , vol.5 , pp. 997-1015
    • Quiocho, F.A.1    Spurlino, J.C.2    Rodseth, L.E.3
  • 45
    • 0027995683 scopus 로고
    • Detection, delineation, measurement, and display of cavities in macromoleclar structures
    • Kleywegt, G. J. & Jones, T. A. (1994). Detection, delineation, measurement, and display of cavities in macromoleclar structures. Acta Crystallog. sect. D, 50, 178-185.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 46
    • 0029016268 scopus 로고
    • Energetic origins of specificity of ligand binding in an interior nonpolar cavity of T4 lysozyme
    • Morton, A., Baase, W. A. & Matthews, B. W. (1995). Energetic origins of specificity of ligand binding in an interior nonpolar cavity of T4 lysozyme. Biochemistry, 34, 8564-8575.
    • (1995) Biochemistry , vol.34 , pp. 8564-8575
    • Morton, A.1    Baase, W.A.2    Matthews, B.W.3
  • 47
    • 0000370241 scopus 로고
    • Xe-129 NMR spectroscopic investigation of the interaction of xenon with ions in aqueous solution
    • McKim, S. & Hinton, J. F. (1993). Xe-129 NMR spectroscopic investigation of the interaction of xenon with ions in aqueous solution. J. Magn. Reson. ser. A, 104, 268-272.
    • (1993) J. Magn. Reson. Ser. A , vol.104 , pp. 268-272
    • McKim, S.1    Hinton, J.F.2
  • 49
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Johnson, B. A. & Blevins, R. A. (1994). NMRView: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR, 4, 603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 50
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX Pipes
    • Delaglio, F., Grzesiek, S., Vuister, G., Zhu, G., Pfeifer, J. & Bax, A. (1995). NMRPipe: a multidimensional spectral processing system based on UNIX Pipes. J. Biomol. NMR, 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 52
    • 4243533658 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4 (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D, 55, 49-81.
    • (1994) Acta Crystallog. Sect. D , vol.55 , pp. 49-81
  • 54
    • 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 Crystallog. sect. A, 47, 110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 55
    • 0000243829 scopus 로고
    • PROCHECK - A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thorton, J. M. (1993). PROCHECK - a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26, 283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thorton, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.