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Volumn 11, Issue 1, 2000, Pages 67-71

Riding the wave: Structural and energetic principles of helical membrane proteins

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 0033956331     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(99)00056-7     Document Type: Review
Times cited : (31)

References (41)
  • 1
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin E., von Heijne G. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 7:1998;1029-1038.
    • (1998) Protein Sci , vol.7 , pp. 1029-1038
    • Wallin, E.1    Von Heijne, G.2
  • 2
    • 0031840579 scopus 로고    scopus 로고
    • G protein-coupled receptors in silico
    • Horn F., Vriend G. G protein-coupled receptors in silico. J Mol Med. 76:1998;464-468.
    • (1998) J Mol Med , vol.76 , pp. 464-468
    • Horn, F.1    Vriend, G.2
  • 3
    • 0030671337 scopus 로고    scopus 로고
    • Orphan G protein-coupled receptors: A neglected opportunity for pioneer drug discovery
    • Stadel J., Wilson S., Bergsma D. Orphan G protein-coupled receptors: a neglected opportunity for pioneer drug discovery. Trends Pharmacol Sci. 18:1997;430-437.
    • (1997) Trends Pharmacol Sci , vol.18 , pp. 430-437
    • Stadel, J.1    Wilson, S.2    Bergsma, D.3
  • 5
    • 0032996996 scopus 로고    scopus 로고
    • Parameters influencing human mu opioid receptor over-expression in baculovirus-infected insect cells
    • Massotte D., Pereira C.A., Pouliquen Y., Pattus F. Parameters influencing human mu opioid receptor over-expression in baculovirus-infected insect cells. J Biotechnol. 69:1999;39-45.
    • (1999) J Biotechnol , vol.69 , pp. 39-45
    • Massotte, D.1    Pereira, C.A.2    Pouliquen, Y.3    Pattus, F.4
  • 6
    • 0030298385 scopus 로고    scopus 로고
    • Heterologous expression of G-protein coupled receptors
    • Tate C.G., Grisshammer R. Heterologous expression of G-protein coupled receptors. Trends Biotechnol. 14:1996;426-430.
    • (1996) Trends Biotechnol , vol.14 , pp. 426-430
    • Tate, C.G.1    Grisshammer, R.2
  • 7
    • 0033580920 scopus 로고    scopus 로고
    • Molecular chaperones stimulate the functional expression of the cocaine-sensitive serotonin transporter
    • Tate C.G., Whiteley E., Betenbaugh M.J. Molecular chaperones stimulate the functional expression of the cocaine-sensitive serotonin transporter. J Biol Chem. 274:1999;17551-17558.
    • (1999) J Biol Chem , vol.274 , pp. 17551-17558
    • Tate, C.G.1    Whiteley, E.2    Betenbaugh, M.J.3
  • 8
    • 0031471216 scopus 로고    scopus 로고
    • Overexpression of a glutamate receptor (GluR2) ligand binding domain in Escherichia coli: Application of novel protein folding screen
    • Chen G.Q., Gouaux E. Overexpression of a glutamate receptor (GluR2) ligand binding domain in Escherichia coli: application of novel protein folding screen. Proc Natl Acad Sci USA. 94:1997;13431-13436.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13431-13436
    • Chen, G.Q.1    Gouaux, E.2
  • 9
    • 0032789940 scopus 로고    scopus 로고
    • A new protein folding screen: Application to the ligand binding domains of a glutamate and kainate receptor and to lysozyme and carbonic anhydrase
    • A screen for protein folding conditions is described. The screen includes 12 factors shown by previous experiments to enhance protein folding and it incorporates the 12 factors into 16 different folding conditions. By examining a 1/256th fraction of the full factorial, multiple folding conditions were determined for several proteins. The impact of each factor on the formation of biologically active material was estimated by calculating the main effects of factors
    • Armstrong N., de Lencastre A., Gouaux E. A new protein folding screen: application to the ligand binding domains of a glutamate and kainate receptor and to lysozyme and carbonic anhydrase. Protein Sci. 8:1999;1475-1483. A screen for protein folding conditions is described. The screen includes 12 factors shown by previous experiments to enhance protein folding and it incorporates the 12 factors into 16 different folding conditions. By examining a 1/256th fraction of the full factorial, multiple folding conditions were determined for several proteins. The impact of each factor on the formation of biologically active material was estimated by calculating the main effects of factors.
    • (1999) Protein Sci , vol.8 , pp. 1475-1483
    • Armstrong, N.1    De Lencastre, A.2    Gouaux, E.3
  • 10
    • 0030451437 scopus 로고    scopus 로고
    • Amphipols: Polymers that keep membrane proteins soluble in aqueous solution
    • Tribet C., Audebert R., Popot J-L. Amphipols: polymers that keep membrane proteins soluble in aqueous solution. Proc Natl Acad Sci USA. 93:1996;15047-15050.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 15047-15050
    • Tribet, C.1    Audebert, R.2    Popot, J.-L.3
  • 11
    • 0033538418 scopus 로고    scopus 로고
    • Changing single side-chains can greatly enhance the resistance of a membrane protein to irreversible inactivation
    • The properties that confer detergent stability to some membrane proteins are unknown. The results presented in this publication demonstrate that stability enhancing mutations can be found relatively frequently in a membrane protein and that individual sidechain substitutions can significantly improve the properties of membrane proteins in detergent solutions. A combination of mutations leads to an even greater enhancement of thermal stability
    • Lau F.W., Nauli S., Zhou Y., Bowie J.U. Changing single side-chains can greatly enhance the resistance of a membrane protein to irreversible inactivation. J Mol Biol. 290:1999;559-564. The properties that confer detergent stability to some membrane proteins are unknown. The results presented in this publication demonstrate that stability enhancing mutations can be found relatively frequently in a membrane protein and that individual sidechain substitutions can significantly improve the properties of membrane proteins in detergent solutions. A combination of mutations leads to an even greater enhancement of thermal stability.
    • (1999) J Mol Biol , vol.290 , pp. 559-564
    • Lau, F.W.1    Nauli, S.2    Zhou, Y.3    Bowie, J.U.4
  • 12
    • 0021181792 scopus 로고
    • A purified alanine carrier composed of a single polypeptide from thermophilic bacterium PS3 driven by either proton or sodium ion gradient
    • Hirata H., Kambe T., Kagawa Y. A purified alanine carrier composed of a single polypeptide from thermophilic bacterium PS3 driven by either proton or sodium ion gradient. J Biol Chem. 259:1984;10653-10656.
    • (1984) J Biol Chem , vol.259 , pp. 10653-10656
    • Hirata, H.1    Kambe, T.2    Kagawa, Y.3
  • 13
    • 0029869003 scopus 로고    scopus 로고
    • Purification and reconstitution of the glutamate carrier GltT of the thermophilic bacterium Bacillus stearothermophilus
    • Gaillard I., Slotboon D-J., Knol J., Lokema J., Konings W. Purification and reconstitution of the glutamate carrier GltT of the thermophilic bacterium Bacillus stearothermophilus. Biochemistry. 35:1996;6150-6156.
    • (1996) Biochemistry , vol.35 , pp. 6150-6156
    • Gaillard, I.1    Slotboon, D.-J.2    Knol, J.3    Lokema, J.4    Konings, W.5
  • 14
    • 0031543433 scopus 로고    scopus 로고
    • G-protein coupled receptors in Saccharomyces cerevisiae: High-throughput screening assays for drug discovery
    • Pausch M.H. G-protein coupled receptors in Saccharomyces cerevisiae: high-throughput screening assays for drug discovery. Trends Biotechnol. 15:1997;487-494.
    • (1997) Trends Biotechnol , vol.15 , pp. 487-494
    • Pausch, M.H.1
  • 15
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • Popot J-L., Engelman D.M. Membrane protein folding and oligomerization: the two-stage model. Biochemistry. 29:1990;4032-4037.
    • (1990) Biochemistry , vol.29 , pp. 4032-4037
    • Popot, J.-L.1    Engelman, D.M.2
  • 16
    • 0040632226 scopus 로고    scopus 로고
    • Membrane protein structure: Variations on the two-stage folding concept
    • in press
    • Popot J-L., Engelman D.M. Membrane protein structure: variations on the two-stage folding concept. Annu Rev Biochem. 69:2000;. in press.
    • (2000) Annu Rev Biochem , vol.69
    • Popot, J.-L.1    Engelman, D.M.2
  • 17
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • Progress toward a detailed understanding of the interactions of membrane proteins in a lipid bilayer environment is summarized in this review by means of a thermodynamic framework for describing membrane protein folding and stability. The framework includes a coherent thermodynamic formalism for determining and describing the energetics of peptide-bilayer interactions and a review of the properties of the environment of membrane proteins
    • White S.H., Wimley W.C. Membrane protein folding and stability: physical principles. Annu Rev Biophys Biomol Struct. 28:1999;319-365. Progress toward a detailed understanding of the interactions of membrane proteins in a lipid bilayer environment is summarized in this review by means of a thermodynamic framework for describing membrane protein folding and stability. The framework includes a coherent thermodynamic formalism for determining and describing the energetics of peptide-bilayer interactions and a review of the properties of the environment of membrane proteins.
    • (1999) Annu Rev Biophys Biomol Struct , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 18
    • 0033514311 scopus 로고    scopus 로고
    • TOXCAT: A measure of transmembrane helix association in a biological membrane
    • The side-to-side association of transmembrane α helices represents a fundamental step in the folding of helical transmembrane proteins. The TOXCAT system provides an improved genetic method for the study of such interactions in a natural membrane environment. Particularly exciting is the potential to genetically discover transmembrane associations from random sequence libraries comprised of hydrophobic stretches
    • Russ W.P., Engelman D.M. TOXCAT: a measure of transmembrane helix association in a biological membrane. Proc Natl Acad Sci USA. 96:1999;863-868. The side-to-side association of transmembrane α helices represents a fundamental step in the folding of helical transmembrane proteins. The TOXCAT system provides an improved genetic method for the study of such interactions in a natural membrane environment. Particularly exciting is the potential to genetically discover transmembrane associations from random sequence libraries comprised of hydrophobic stretches.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 863-868
    • Russ, W.P.1    Engelman, D.M.2
  • 19
    • 0030575833 scopus 로고    scopus 로고
    • Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator
    • Langosch D., Brosig B., Kolmar H., Fritz H-J. Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator. J Mol Biol. 263:1996;525-530.
    • (1996) J Mol Biol , vol.263 , pp. 525-530
    • Langosch, D.1    Brosig, B.2    Kolmar, H.3    Fritz, H.-J.4
  • 20
    • 0033582936 scopus 로고    scopus 로고
    • Transmembrane structure of an inwardly rectifying potassium channel
    • A yeast genetic screen is used to identify functional channels from libraries containing mutagenized transmembrane domains. Protein-lipid and protein-water interaction surfaces were identified by the patterns of observed allowed sequences, and a model for the channel is proposed in which the arrangement of the transmembrane helices is distinctly different from the structure of a bacterial potassium channel with the same topology. The method may be used to obtain structural information in the absence of a high-resolution structure
    • Minor D.L. Jr., Masseling S.J., Jan Y.N., Jan L.Y. Transmembrane structure of an inwardly rectifying potassium channel. Cell. 96:1999;879-891. A yeast genetic screen is used to identify functional channels from libraries containing mutagenized transmembrane domains. Protein-lipid and protein-water interaction surfaces were identified by the patterns of observed allowed sequences, and a model for the channel is proposed in which the arrangement of the transmembrane helices is distinctly different from the structure of a bacterial potassium channel with the same topology. The method may be used to obtain structural information in the absence of a high-resolution structure.
    • (1999) Cell , vol.96 , pp. 879-891
    • Minor D.L., Jr.1    Masseling, S.J.2    Jan, Y.N.3    Jan, L.Y.4
  • 22
    • 0029811389 scopus 로고    scopus 로고
    • Analysis of hydrophobic proteins and peptides by electrospray ionization MS
    • Fearnley I.M., Walker J.E. Analysis of hydrophobic proteins and peptides by electrospray ionization MS. Biochem Soc Trans. 24:1996;912-917.
    • (1996) Biochem Soc Trans , vol.24 , pp. 912-917
    • Fearnley, I.M.1    Walker, J.E.2
  • 23
    • 0032873674 scopus 로고    scopus 로고
    • Toward the bilayer proteome, electrospray ionization-mass spectrometry of large, intact transmembrane proteins
    • This study demonstrates the successful application of ESI-MS technology to full-length lactose permease, a membrane protein containing 12 transmembrane α-helical domains
    • Whitelegge J.P., le Coutre J., Lee J.C., Engel C.K., Prive G.G., Faull K.F., Kaback H.R. Toward the bilayer proteome, electrospray ionization-mass spectrometry of large, intact transmembrane proteins. Proc Natl Acad Sci USA. 96:1999;10695-10698. This study demonstrates the successful application of ESI-MS technology to full-length lactose permease, a membrane protein containing 12 transmembrane α-helical domains.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10695-10698
    • Whitelegge, J.P.1    Le Coutre, J.2    Lee, J.C.3    Engel, C.K.4    Prive, G.G.5    Faull, K.F.6    Kaback, H.R.7
  • 24
    • 0032168447 scopus 로고    scopus 로고
    • Cysteine reactivity and oligomeric structures of phospholamban and its mutants
    • Karim C.B., Stamm J.D., Karim J., Jones L.R., Thomas D.D. Cysteine reactivity and oligomeric structures of phospholamban and its mutants. Biochemistry. 37:1998;12074-12081.
    • (1998) Biochemistry , vol.37 , pp. 12074-12081
    • Karim, C.B.1    Stamm, J.D.2    Karim, J.3    Jones, L.R.4    Thomas, D.D.5
  • 25
    • 0032988826 scopus 로고    scopus 로고
    • A fluorescence energy transfer method for analyzing protein oligomeric structure: Application to phospholamban
    • Li M., Reddy L.G., Bennett R., Silva N.D. Jr., Jones L.R., Thomas D.D. A fluorescence energy transfer method for analyzing protein oligomeric structure: application to phospholamban. Biophys J. 76:1999;2587-2599.
    • (1999) Biophys J , vol.76 , pp. 2587-2599
    • Li, M.1    Reddy, L.G.2    Bennett, R.3    Silva N.D., Jr.4    Jones, L.R.5    Thomas, D.D.6
  • 26
    • 0033616627 scopus 로고    scopus 로고
    • Depolymerization of phospholamban in the presence of calcium pump: A fluorescence energy transfer study
    • Reddy L.G., Jones L.R., Thomas D.D. Depolymerization of phospholamban in the presence of calcium pump: a fluorescence energy transfer study. Biochemistry. 38:1999;3954-3962.
    • (1999) Biochemistry , vol.38 , pp. 3954-3962
    • Reddy, L.G.1    Jones, L.R.2    Thomas, D.D.3
  • 27
    • 0033583036 scopus 로고    scopus 로고
    • Co-reconstitution of phospholamban mutants with the Ca-ATPase reveals dependence of inhibitory function on phospholamban structure
    • Reddy L.G., Autry J.M., Jones L.R., Thomas D.D. Co-reconstitution of phospholamban mutants with the Ca-ATPase reveals dependence of inhibitory function on phospholamban structure. J Biol Chem. 274:1999;7649-7655.
    • (1999) J Biol Chem , vol.274 , pp. 7649-7655
    • Reddy, L.G.1    Autry, J.M.2    Jones, L.R.3    Thomas, D.D.4
  • 29
    • 0030777759 scopus 로고    scopus 로고
    • The effect of point mutations on the free energy of transmembrane α-helix dimerization
    • Fleming K.G., Ackerman A.L., Engelman D.M. The effect of point mutations on the free energy of transmembrane α-helix dimerization. J Mol Biol. 272:1997;266-275.
    • (1997) J Mol Biol , vol.272 , pp. 266-275
    • Fleming, K.G.1    Ackerman, A.L.2    Engelman, D.M.3
  • 30
    • 0032984921 scopus 로고    scopus 로고
    • Modern applications of the analytical ultracentrifuge
    • Laue T.M., Stafford W.M. Modern applications of the analytical ultracentrifuge. Annu Rev Biophys Biomol Struct. 28:1999;75-100.
    • (1999) Annu Rev Biophys Biomol Struct , vol.28 , pp. 75-100
    • Laue, T.M.1    Stafford, W.M.2
  • 31
    • 0033580880 scopus 로고    scopus 로고
    • Structure of the Escherichia coli fumarate reductase respiratory complex
    • Iverson T.M., Luna-Chavez C., Cecchini G., Rees D.C. Structure of the Escherichia coli fumarate reductase respiratory complex. Science. 284:1999;1961-1966.
    • (1999) Science , vol.284 , pp. 1961-1966
    • Iverson, T.M.1    Luna-Chavez, C.2    Cecchini, G.3    Rees, D.C.4
  • 33
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • Chang G., Spencer R.H., Lee A.T., Barclay M.T., Rees D.C. Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science. 282:1998;2220-2226.
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 35
    • 0033567092 scopus 로고    scopus 로고
    • Protein, lipid and water organization in bacteriorhodopsin crystals: A molecular view of the purple membrane at 1.9 angstrom resolution
    • Belrhali H., Nollert P., Royant A., Menzel C., Rosenbusch J.P., Landau E.M., Pebay-Peyroula E. Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 angstrom resolution. Structure Fold Des. 7:1999;909-917.
    • (1999) Structure Fold des , vol.7 , pp. 909-917
    • Belrhali, H.1    Nollert, P.2    Royant, A.3    Menzel, C.4    Rosenbusch, J.P.5    Landau, E.M.6    Pebay-Peyroula, E.7
  • 36
    • 0032518244 scopus 로고    scopus 로고
    • It's not just a phase: Crystallization and X-ray structure determination of bacteriorhodopsin in lipidic cubic phases
    • Gouaux E. It's not just a phase: crystallization and X-ray structure determination of bacteriorhodopsin in lipidic cubic phases. Structure. 6:1998;5-10.
    • (1998) Structure , vol.6 , pp. 5-10
    • Gouaux, E.1
  • 37
    • 0031829172 scopus 로고    scopus 로고
    • Lipidic cubic phases: New matrices for the three-dimensional crystallization of membrane proteins
    • The phenomenology of bicontinuous cubic phases is presented. Detailed prescriptions of the preparation of lipidic cubic phase matrices are given and their potential for the crystallization of other biological macromolecules is discussed
    • Rummel G., Hardmeyer A., Widmer C., Chiu M.L., Nollert P., Locher K.P., Pedruzzi I., Landau E.M., Rosenbusch J.P. Lipidic cubic phases: new matrices for the three-dimensional crystallization of membrane proteins. J Struct Biol. 121:1998;82-91. The phenomenology of bicontinuous cubic phases is presented. Detailed prescriptions of the preparation of lipidic cubic phase matrices are given and their potential for the crystallization of other biological macromolecules is discussed.
    • (1998) J Struct Biol , vol.121 , pp. 82-91
    • Rummel, G.1    Hardmeyer, A.2    Widmer, C.3    Chiu, M.L.4    Nollert, P.5    Locher, K.P.6    Pedruzzi, I.7    Landau, E.M.8    Rosenbusch, J.P.9
  • 39
    • 0033536594 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution
    • Understanding the mechanism whereby bacteriorhodopsin orchestrates the unidirectional translocation of a proton across a membrane requires a description of the structural changes that occur during the photocycle. The structure of the M state reveals structural clues that suggest a means for conserving energy at the active site and for ensuring the directionality of the proton translocation. Importantly, the solution of the structure of this photocycle intermediate, made possible through the use of bicontinuous cubic lipid phases in the crystallization matrix, represents the initiation of a structure-function cycle for probing the details on how bacteriorhodopsin couples the isomerization of retinal to the transmembrane movement of ions
    • Luecke H., Schobert B., Richter H-T., Cartailler J-P., Lanyi J.K. Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution. Science. 286:1999;255-260. Understanding the mechanism whereby bacteriorhodopsin orchestrates the unidirectional translocation of a proton across a membrane requires a description of the structural changes that occur during the photocycle. The structure of the M state reveals structural clues that suggest a means for conserving energy at the active site and for ensuring the directionality of the proton translocation. Importantly, the solution of the structure of this photocycle intermediate, made possible through the use of bicontinuous cubic lipid phases in the crystallization matrix, represents the initiation of a structure-function cycle for probing the details on how bacteriorhodopsin couples the isomerization of retinal to the transmembrane movement of ions.
    • (1999) Science , vol.286 , pp. 255-260
    • Luecke, H.1    Schobert, B.2    Richter, H.-T.3    Cartailler, J.-P.4    Lanyi, J.K.5
  • 40
    • 0029671464 scopus 로고    scopus 로고
    • Engineering the lac permease for purification and crystallization
    • Prive G.G., Kaback H.R. Engineering the lac permease for purification and crystallization. J Bioenerg Biomembr. 28:1996;29-34.
    • (1996) J Bioenerg Biomembr , vol.28 , pp. 29-34
    • Prive, G.G.1    Kaback, H.R.2


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