메뉴 건너뛰기




Volumn 375, Issue 5, 2008, Pages 1258-1266

Examining the Dynamic Energy Landscape of an Antiporter upon Inhibitor Binding

Author keywords

atomic force microscopy; Na+ H+ antiporter of Escherichia coli; NhaA; single molecule force spectroscopy; SMFS

Indexed keywords

AMINOPERIMIDINE; PROTEIN INHIBITOR; PROTEIN NHAA; SODIUM PROTON EXCHANGE PROTEIN; UNCLASSIFIED DRUG;

EID: 37549016432     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.11.032     Document Type: Article
Times cited : (29)

References (46)
  • 1
    • 0032504237 scopus 로고    scopus 로고
    • G protein-coupled receptors: I. Diversity of receptor-ligand interactions
    • Ji T.H., Grossmann M., and Ji I.H. G protein-coupled receptors: I. Diversity of receptor-ligand interactions. J. Biol. Chem. 273 (1998) 17299-17302
    • (1998) J. Biol. Chem. , vol.273 , pp. 17299-17302
    • Ji, T.H.1    Grossmann, M.2    Ji, I.H.3
  • 3
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder H., Sligar S.G., and Wolynes P.G. The energy landscapes and motions of proteins. Science 254 (1991) 1598-1603
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 4
    • 0030867610 scopus 로고    scopus 로고
    • Ligand binding to proteins: the binding landscape model
    • Miller D.W., and Dill K.A. Ligand binding to proteins: the binding landscape model. Protein Sci. 6 (1997) 2166-2179
    • (1997) Protein Sci. , vol.6 , pp. 2166-2179
    • Miller, D.W.1    Dill, K.A.2
  • 5
    • 0033056708 scopus 로고    scopus 로고
    • Folding funnels, binding funnels, and protein function
    • Tsai C.J., Kumar S., Ma B., and Nussinov R. Folding funnels, binding funnels, and protein function. Protein Sci. 8 (1999) 1181-1190
    • (1999) Protein Sci. , vol.8 , pp. 1181-1190
    • Tsai, C.J.1    Kumar, S.2    Ma, B.3    Nussinov, R.4
  • 6
    • 0028309424 scopus 로고
    • Adhesion forces between individual ligand-receptor pairs
    • Florin E.L., Moy V.T., and Gaub H.E. Adhesion forces between individual ligand-receptor pairs. Science 264 (1994) 415-417
    • (1994) Science , vol.264 , pp. 415-417
    • Florin, E.L.1    Moy, V.T.2    Gaub, H.E.3
  • 7
    • 0028007197 scopus 로고
    • Direct measurement of the forces between complementary strands of DNA
    • Lee G.U., Chrisey L.A., and Colton R.J. Direct measurement of the forces between complementary strands of DNA. Science 266 (1994) 771-773
    • (1994) Science , vol.266 , pp. 771-773
    • Lee, G.U.1    Chrisey, L.A.2    Colton, R.J.3
  • 9
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief M., Gautel M., Oesterhelt F., Fernandez J.M., and Gaub H.E. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 267 (1997) 1109-1112
    • (1997) Science , vol.267 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 10
    • 0033772174 scopus 로고    scopus 로고
    • Discrete interactions in cell adhesion measured by single-molecule force spectroscopy
    • Benoit M., Gabriel D., Gerisch G., and Gaub H.E. Discrete interactions in cell adhesion measured by single-molecule force spectroscopy. Nat. Cell Biol. 2 (2000) 313-317
    • (2000) Nat. Cell Biol. , vol.2 , pp. 313-317
    • Benoit, M.1    Gabriel, D.2    Gerisch, G.3    Gaub, H.E.4
  • 11
    • 34249936024 scopus 로고    scopus 로고
    • Forces and bond dynamics in cell adhesion
    • Evans E.A., and Calderwood D.A. Forces and bond dynamics in cell adhesion. Science 316 (2007) 1148-1153
    • (2007) Science , vol.316 , pp. 1148-1153
    • Evans, E.A.1    Calderwood, D.A.2
  • 12
    • 0033817704 scopus 로고    scopus 로고
    • Stretching single molecules into novel conformations using the atomic force microscope
    • Fisher T.E., Marszalek P.E., and Fernandez J.M. Stretching single molecules into novel conformations using the atomic force microscope. Nat. Struct. Biol. 7 (2000) 719-724
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 719-724
    • Fisher, T.E.1    Marszalek, P.E.2    Fernandez, J.M.3
  • 13
    • 34347259478 scopus 로고    scopus 로고
    • Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy
    • Kedrov A., Janovjak H., Sapra K.T., and Müller D.J. Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy. Annu. Rev. Biophys. Biomol. Struct. 36 (2007) 233-260
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 233-260
    • Kedrov, A.1    Janovjak, H.2    Sapra, K.T.3    Müller, D.J.4
  • 15
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell G.I. Models for the specific adhesion of cells to cells. Science 200 (1978) 618-627
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 16
    • 0032227720 scopus 로고    scopus 로고
    • Energy landscapes of biomolecular adhesion and receptor anchoring at interfaces explored with dynamic force spectroscopy
    • Evans E. Energy landscapes of biomolecular adhesion and receptor anchoring at interfaces explored with dynamic force spectroscopy. Faraday Discuss. (1998) 1-16
    • (1998) Faraday Discuss. , pp. 1-16
    • Evans, E.1
  • 17
    • 11844275345 scopus 로고    scopus 로고
    • 2-Aminoperimidine, a specific inhibitor of bacterial NhaA Na(+)/H(+) antiporters
    • Dibrov P., Rimon A., Dzioba J., Winogrodzki A., Shalitin Y., and Padan E. 2-Aminoperimidine, a specific inhibitor of bacterial NhaA Na(+)/H(+) antiporters. FEBS Lett. 579 (2005) 373-378
    • (2005) FEBS Lett. , vol.579 , pp. 373-378
    • Dibrov, P.1    Rimon, A.2    Dzioba, J.3    Winogrodzki, A.4    Shalitin, Y.5    Padan, E.6
  • 20
    • 3242796697 scopus 로고    scopus 로고
    • Controlled unfolding and refolding of a single sodium-proton antiporter using atomic force microscopy
    • Kedrov A., Ziegler C., Janovjak H., Kühlbrandt W., and Müller D.J. Controlled unfolding and refolding of a single sodium-proton antiporter using atomic force microscopy. J. Mol. Biol. 340 (2004) 1143-1152
    • (2004) J. Mol. Biol. , vol.340 , pp. 1143-1152
    • Kedrov, A.1    Ziegler, C.2    Janovjak, H.3    Kühlbrandt, W.4    Müller, D.J.5
  • 22
    • 0141753133 scopus 로고    scopus 로고
    • Unfolding pathways of native bacteriorhodopsin depend on temperature
    • Janovjak H., Kessler M., Oesterhelt D., Gaub H., and Müller D.J. Unfolding pathways of native bacteriorhodopsin depend on temperature. EMBO J. 22 (2003) 5220-5229
    • (2003) EMBO J. , vol.22 , pp. 5220-5229
    • Janovjak, H.1    Kessler, M.2    Oesterhelt, D.3    Gaub, H.4    Müller, D.J.5
  • 23
    • 29144532994 scopus 로고    scopus 로고
    • Characterizing molecular interactions in different bacteriorhodopsin assemblies by single-molecule force spectroscopy
    • Sapra K.T., Besir H., Oesterhelt D., and Müller D.J. Characterizing molecular interactions in different bacteriorhodopsin assemblies by single-molecule force spectroscopy. J. Mol. Biol. 355 (2006) 640-650
    • (2006) J. Mol. Biol. , vol.355 , pp. 640-650
    • Sapra, K.T.1    Besir, H.2    Oesterhelt, D.3    Müller, D.J.4
  • 25
    • 33748467970 scopus 로고    scopus 로고
    • Differentiating ligand and inhibitor interactions of a single antiporter
    • Kedrov A., Ziegler C., and Müller D.J. Differentiating ligand and inhibitor interactions of a single antiporter. J. Mol. Biol. 362 (2006) 925-932
    • (2006) J. Mol. Biol. , vol.362 , pp. 925-932
    • Kedrov, A.1    Ziegler, C.2    Müller, D.J.3
  • 28
    • 9744250110 scopus 로고    scopus 로고
    • Strength of integration of transmembrane alpha-helical peptides in lipid bilayers as determined by atomic force microscopy
    • Ganchev D., Rijkers D., Snel M., Killian J., and de Kruijff B. Strength of integration of transmembrane alpha-helical peptides in lipid bilayers as determined by atomic force microscopy. Biochemistry 43 (2004) 14987-14993
    • (2004) Biochemistry , vol.43 , pp. 14987-14993
    • Ganchev, D.1    Rijkers, D.2    Snel, M.3    Killian, J.4    de Kruijff, B.5
  • 29
    • 33846264595 scopus 로고    scopus 로고
    • Transmembrane helices have rough energy surfaces
    • Janovjak H., Knaus H., and Müller D.J. Transmembrane helices have rough energy surfaces. J. Am. Chem. Soc. 129 (2007) 246-247
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 246-247
    • Janovjak, H.1    Knaus, H.2    Müller, D.J.3
  • 30
    • 0034979287 scopus 로고    scopus 로고
    • Probing the relation between force-lifetime-and chemistry in single molecular bonds
    • Evans E. Probing the relation between force-lifetime-and chemistry in single molecular bonds. Annu. Rev. Biophys. Biomol. Struct. 30 (2001) 105-128
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 105-128
    • Evans, E.1
  • 32
    • 0030943892 scopus 로고    scopus 로고
    • Binding of ligand or monoclonal antibody 4B1 induces discrete structural changes in the lactose permease of Escherichia coli
    • Frillingos S., Wu J., Venkatesan P., and Kaback H.R. Binding of ligand or monoclonal antibody 4B1 induces discrete structural changes in the lactose permease of Escherichia coli. Biochemistry 36 (1997) 6408-6414
    • (1997) Biochemistry , vol.36 , pp. 6408-6414
    • Frillingos, S.1    Wu, J.2    Venkatesan, P.3    Kaback, H.R.4
  • 33
    • 0033621118 scopus 로고    scopus 로고
    • The propagation of binding interactions to remote sites in proteins: analysis of the binding of the monoclonal antibody D1.3 to lysozyme
    • Freire E. The propagation of binding interactions to remote sites in proteins: analysis of the binding of the monoclonal antibody D1.3 to lysozyme. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 10118-10122
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 10118-10122
    • Freire, E.1
  • 34
    • 34147138772 scopus 로고    scopus 로고
    • Dwell-time distribution analysis of polyprotein unfolding using force-clamp spectroscopy
    • Brujic J., Hermans R.I., Garcia-Manyes S., Walther K.A., and Fernandez J.M. Dwell-time distribution analysis of polyprotein unfolding using force-clamp spectroscopy. Biophys. J. 92 (2007) 2896-2903
    • (2007) Biophys. J. , vol.92 , pp. 2896-2903
    • Brujic, J.1    Hermans, R.I.2    Garcia-Manyes, S.3    Walther, K.A.4    Fernandez, J.M.5
  • 36
    • 0033970020 scopus 로고    scopus 로고
    • Folding and binding cascades: dynamic landscapes and population shifts
    • Kumar S., Ma B., Tsai C.J., Sinha N., and Nussinov R. Folding and binding cascades: dynamic landscapes and population shifts. Protein Sci. 9 (2000) 10-19
    • (2000) Protein Sci. , vol.9 , pp. 10-19
    • Kumar, S.1    Ma, B.2    Tsai, C.J.3    Sinha, N.4    Nussinov, R.5
  • 37
    • 33747592347 scopus 로고    scopus 로고
    • The experimental survey of protein-folding energy landscapes
    • Oliveberg M., and Wolynes P.G. The experimental survey of protein-folding energy landscapes. Q. Rev. Biophys. 38 (2005) 245-288
    • (2005) Q. Rev. Biophys. , vol.38 , pp. 245-288
    • Oliveberg, M.1    Wolynes, P.G.2
  • 38
    • 0033531109 scopus 로고    scopus 로고
    • Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy
    • Merkel R., Nassoy P., Leung A., Ritchie K., and Evans E. Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature 397 (1999) 50-53
    • (1999) Nature , vol.397 , pp. 50-53
    • Merkel, R.1    Nassoy, P.2    Leung, A.3    Ritchie, K.4    Evans, E.5
  • 39
    • 30644476474 scopus 로고    scopus 로고
    • Dynamic force spectroscopy of the digoxigenin-antibody complex
    • Neuert G., Albrecht C., Pamir E., and Gaub H.E. Dynamic force spectroscopy of the digoxigenin-antibody complex. FEBS Lett. 580 (2006) 505-509
    • (2006) FEBS Lett. , vol.580 , pp. 505-509
    • Neuert, G.1    Albrecht, C.2    Pamir, E.3    Gaub, H.E.4
  • 40
    • 34447299432 scopus 로고    scopus 로고
    • Energy landscape of chelated uranyl-antibody interactions by dynamic force spectroscopy
    • Odorico M., Teulon J.M., Bessou T., Vidaud C., Bellanger L., Chen S.W., et al. Energy landscape of chelated uranyl-antibody interactions by dynamic force spectroscopy. Biophys. J. 93 (2007) 645-654
    • (2007) Biophys. J. , vol.93 , pp. 645-654
    • Odorico, M.1    Teulon, J.M.2    Bessou, T.3    Vidaud, C.4    Bellanger, L.5    Chen, S.W.6
  • 41
    • 33847755180 scopus 로고    scopus 로고
    • Dynamic force spectroscopy of the specific interaction between the PDZ domain and its recognition peptides
    • Maki T., Kidoaki S., Usui K., Suzuki H., Ito M., Ito F., et al. Dynamic force spectroscopy of the specific interaction between the PDZ domain and its recognition peptides. Langmuir 23 (2007) 2668-2673
    • (2007) Langmuir , vol.23 , pp. 2668-2673
    • Maki, T.1    Kidoaki, S.2    Usui, K.3    Suzuki, H.4    Ito, M.5    Ito, F.6
  • 43
    • 37549044937 scopus 로고    scopus 로고
    • Mechanical properties of bovine rhodopsin and bacteriorhodopsin dictate energy landscape and guide conformational changes
    • In revision
    • Sapra K.T., Park P.S., Palczewski K., and Müller D.J. Mechanical properties of bovine rhodopsin and bacteriorhodopsin dictate energy landscape and guide conformational changes. Langmuir (2007) In revision
    • (2007) Langmuir
    • Sapra, K.T.1    Park, P.S.2    Palczewski, K.3    Müller, D.J.4
  • 44
    • 33748468214 scopus 로고
    • The indirect spectrophotometric determination of sulphate with 2-aminoperimidine hydrochloride
    • Burns D.T., Coy J.S., Hayes W.P., and Kent D.M. The indirect spectrophotometric determination of sulphate with 2-aminoperimidine hydrochloride. Microchim. Acta 62 (1974) 245-248
    • (1974) Microchim. Acta , vol.62 , pp. 245-248
    • Burns, D.T.1    Coy, J.S.2    Hayes, W.P.3    Kent, D.M.4
  • 45
    • 0033168715 scopus 로고    scopus 로고
    • Projection structure of NhaA, a secondary transporter from Escherichia coli, at 4.0 Å resolution
    • Williams K.A., Geldmacher-Kaufer U., Padan E., Schuldiner S., and Kühlbrandt W. Projection structure of NhaA, a secondary transporter from Escherichia coli, at 4.0 Å resolution. EMBO J. 18 (1999) 3558-3563
    • (1999) EMBO J. , vol.18 , pp. 3558-3563
    • Williams, K.A.1    Geldmacher-Kaufer, U.2    Padan, E.3    Schuldiner, S.4    Kühlbrandt, W.5
  • 46
    • 34347209835 scopus 로고
    • Calculation of thermal noise in atomic force microscopy
    • Butt H.J., and Jaschke M. Calculation of thermal noise in atomic force microscopy. Nanotechnology 6 (1995) 1-7
    • (1995) Nanotechnology , vol.6 , pp. 1-7
    • Butt, H.J.1    Jaschke, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.