메뉴 건너뛰기




Volumn 581, Issue 7, 2007, Pages 1335-1341

Membrane protein assembly patterns reflect selection for non-proliferative structures

Author keywords

Classification; Membrane protein; Protein folding; Quaternary protein structure

Indexed keywords

CARRIER PROTEIN; MEMBRANE PROTEIN; MONOMER; OLIGOMER; POLYPEPTIDE;

EID: 33947380200     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.02.050     Document Type: Article
Times cited : (13)

References (44)
  • 1
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin E., and 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
    • 1542723470 scopus 로고    scopus 로고
    • Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism
    • Liu Y., Gerstein M., and Engelman D.M. Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism. Proc. Natl. Acad. Sci. USA 101 (2004) 3495-3497
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3495-3497
    • Liu, Y.1    Gerstein, M.2    Engelman, D.M.3
  • 3
    • 1542376209 scopus 로고    scopus 로고
    • Missense mutations in transmembrane domains of proteins: phenotypic propensity of polar residues for human disease
    • Partridge A.W., Therien A.G., and Deber C.M. Missense mutations in transmembrane domains of proteins: phenotypic propensity of polar residues for human disease. Proteins 54 (2004) 648-656
    • (2004) Proteins , vol.54 , pp. 648-656
    • Partridge, A.W.1    Therien, A.G.2    Deber, C.M.3
  • 4
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: the two-stage model
    • Popot J.L., and Engelman D.M. Membrane protein folding and oligomerization: the two-stage model. Biochemistry 29 (1990) 4031-4037
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 5
    • 0037379072 scopus 로고    scopus 로고
    • How do helix-helix interactions help determine the folds of membrane proteins? Perspectives from the study of homo-oligomeric helical bundles
    • DeGrado W.F., Gratkowski H., and Lear J.D. How do helix-helix interactions help determine the folds of membrane proteins? Perspectives from the study of homo-oligomeric helical bundles. Protein Sci. 12 (2003) 647-665
    • (2003) Protein Sci. , vol.12 , pp. 647-665
    • DeGrado, W.F.1    Gratkowski, H.2    Lear, J.D.3
  • 6
    • 0242657348 scopus 로고    scopus 로고
    • Membrane protein folding: beyond the two stage model
    • Engelman D.M., et al. Membrane protein folding: beyond the two stage model. FEBS Lett. 555 (2003) 122-125
    • (2003) FEBS Lett. , vol.555 , pp. 122-125
    • Engelman, D.M.1
  • 7
    • 28444488355 scopus 로고    scopus 로고
    • Solving the membrane protein folding problem
    • Bowie J.U. Solving the membrane protein folding problem. Nature 438 (2005) 581-589
    • (2005) Nature , vol.438 , pp. 581-589
    • Bowie, J.U.1
  • 8
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25 (1997) 4876-4882
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 10
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • Long S.B., Campbell E.B., and Mackinnon R. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 309 (2005) 897-903
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 11
    • 0003742069 scopus 로고
    • Department of Biochemistry and Molecular Biology, University College London
    • Hubbard S.J., and Thornton J.M. 'NACCESS', Computer Program (1993), Department of Biochemistry and Molecular Biology, University College London
    • (1993) 'NACCESS', Computer Program
    • Hubbard, S.J.1    Thornton, J.M.2
  • 12
    • 33746082078 scopus 로고    scopus 로고
    • Lipid solvation effects contribute to the affinity of Gly-xxx-Gly motif-mediated helix-helix interactions
    • Johnson R.M., Rath A., Melnyk R.A., and Deber C.M. Lipid solvation effects contribute to the affinity of Gly-xxx-Gly motif-mediated helix-helix interactions. Biochemistry 45 (2006) 8507-8515
    • (2006) Biochemistry , vol.45 , pp. 8507-8515
    • Johnson, R.M.1    Rath, A.2    Melnyk, R.A.3    Deber, C.M.4
  • 13
    • 33644850534 scopus 로고    scopus 로고
    • Crystal structure of AqpZ tetramer reveals two distinct Arg-189 conformations associated with water permeation through the narrowest constriction of the water-conducting channel
    • Jiang J., Daniels B.V., and Fu D. Crystal structure of AqpZ tetramer reveals two distinct Arg-189 conformations associated with water permeation through the narrowest constriction of the water-conducting channel. J. Biol. Chem. 281 (2006) 454-460
    • (2006) J. Biol. Chem. , vol.281 , pp. 454-460
    • Jiang, J.1    Daniels, B.V.2    Fu, D.3
  • 14
    • 0032817780 scopus 로고    scopus 로고
    • Helix packing in polytopic membrane proteins: role of glycine in transmembrane helix association
    • Javadpour M.M., Eilers M., Groesbeek M., and Smith S.O. Helix packing in polytopic membrane proteins: role of glycine in transmembrane helix association. Biophys. J. 77 (1999) 1609-1618
    • (1999) Biophys. J. , vol.77 , pp. 1609-1618
    • Javadpour, M.M.1    Eilers, M.2    Groesbeek, M.3    Smith, S.O.4
  • 15
    • 0000338489 scopus 로고
    • Comparison of solvent-inaccessible cores of homologous proteins: definitions useful for protein modelling
    • Hubbard T.J., and Blundell T.L. Comparison of solvent-inaccessible cores of homologous proteins: definitions useful for protein modelling. Protein Eng. 1 (1987) 159-171
    • (1987) Protein Eng. , vol.1 , pp. 159-171
    • Hubbard, T.J.1    Blundell, T.L.2
  • 16
    • 28044467526 scopus 로고    scopus 로고
    • Mutagenesis-based definitions and probes of residue burial in proteins
    • Bajaj K., Chakrabarti P., and Varadarajan R. Mutagenesis-based definitions and probes of residue burial in proteins. Proc. Natl. Acad. Sci. USA 102 (2005) 16221-16226
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 16221-16226
    • Bajaj, K.1    Chakrabarti, P.2    Varadarajan, R.3
  • 17
    • 0037136435 scopus 로고    scopus 로고
    • Genomic analysis of membrane protein families: abundance and conserved motifs
    • (research0054)
    • Liu Y., Engelman D.M., and Gerstein M. Genomic analysis of membrane protein families: abundance and conserved motifs. Genome Biol. 3 (2002) (research0054)
    • (2002) Genome Biol. , vol.3
    • Liu, Y.1    Engelman, D.M.2    Gerstein, M.3
  • 18
    • 4143085058 scopus 로고    scopus 로고
    • Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs
    • Senes A., Engel D.E., and DeGrado W.F. Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs. Curr. Opin. Struct. Biol. 14 (2004) 465-479
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 465-479
    • Senes, A.1    Engel, D.E.2    DeGrado, W.F.3
  • 19
    • 0029860263 scopus 로고    scopus 로고
    • Flux coupling in a neuronal glutamate transporter
    • Zerangue N., and Kavanaugh M.P. Flux coupling in a neuronal glutamate transporter. Nature 383 (1996) 634-637
    • (1996) Nature , vol.383 , pp. 634-637
    • Zerangue, N.1    Kavanaugh, M.P.2
  • 20
    • 0029076899 scopus 로고
    • An excitatory amino-acid transporter with properties of a ligand-gated chloride channel
    • Fairman W.A., Vandenberg R.J., Arriza J.L., Kavanaugh M.P., and Amara S.G. An excitatory amino-acid transporter with properties of a ligand-gated chloride channel. Nature 375 (1995) 599-603
    • (1995) Nature , vol.375 , pp. 599-603
    • Fairman, W.A.1    Vandenberg, R.J.2    Arriza, J.L.3    Kavanaugh, M.P.4    Amara, S.G.5
  • 21
    • 7244254186 scopus 로고    scopus 로고
    • Structure of a glutamate transporter homologue from Pyrococcus horikoshii
    • Yernool D., Boudker O., Jin Y., and Gouaux E. Structure of a glutamate transporter homologue from Pyrococcus horikoshii. Nature 431 (2004) 811-818
    • (2004) Nature , vol.431 , pp. 811-818
    • Yernool, D.1    Boudker, O.2    Jin, Y.3    Gouaux, E.4
  • 22
    • 0035943429 scopus 로고    scopus 로고
    • Helix-helix packing and interfacial pairwise interactions of residues in membrane proteins
    • Adamian L., and Liang J. Helix-helix packing and interfacial pairwise interactions of residues in membrane proteins. J. Mol. Biol. 311 (2001) 891-907
    • (2001) J. Mol. Biol. , vol.311 , pp. 891-907
    • Adamian, L.1    Liang, J.2
  • 23
    • 0042931286 scopus 로고    scopus 로고
    • Sequence motifs, polar interactions and conformational changes in helical membrane proteins
    • Curran A.R., and Engelman D.M. Sequence motifs, polar interactions and conformational changes in helical membrane proteins. Curr. Opin. Struct. Biol. 13 (2003) 412-417
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 412-417
    • Curran, A.R.1    Engelman, D.M.2
  • 24
    • 0034327611 scopus 로고    scopus 로고
    • Hinges, swivels and switches: the role of prolines in signalling via transmembrane alpha-helices
    • Sansom M.S., and Weinstein H. Hinges, swivels and switches: the role of prolines in signalling via transmembrane alpha-helices. Trends Pharmacol. Sci. 21 (2000) 445-451
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 445-451
    • Sansom, M.S.1    Weinstein, H.2
  • 25
    • 0024165905 scopus 로고
    • Phospholamban forms Ca2+-selective channels in lipid bilayers
    • Kovacs R.J., Nelson M.T., Simmerman H.K., and Jones L.R. Phospholamban forms Ca2+-selective channels in lipid bilayers. J. Biol. Chem. 263 (1988) 18364-18368
    • (1988) J. Biol. Chem. , vol.263 , pp. 18364-18368
    • Kovacs, R.J.1    Nelson, M.T.2    Simmerman, H.K.3    Jones, L.R.4
  • 27
    • 23344441824 scopus 로고    scopus 로고
    • The structure of phospholamban pentamer reveals a channel-like architecture in membranes
    • Oxenoid K., and Chou J.J. The structure of phospholamban pentamer reveals a channel-like architecture in membranes. Proc. Natl. Acad. Sci. USA 102 (2005) 10870-10875
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10870-10875
    • Oxenoid, K.1    Chou, J.J.2
  • 29
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity
    • Dutzler R., Campbell E.B., Cadene M., Chait B.T., and MacKinnon R. X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity. Nature 415 (2002) 287-294
    • (2002) Nature , vol.415 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 30
    • 28544453561 scopus 로고    scopus 로고
    • Principles of selective ion transport in channels and pumps
    • Gouaux E., and Mackinnon R. Principles of selective ion transport in channels and pumps. Science 310 (2005) 1461-1465
    • (2005) Science , vol.310 , pp. 1461-1465
    • Gouaux, E.1    Mackinnon, R.2
  • 31
    • 33744965940 scopus 로고    scopus 로고
    • Evidence for assembly of small multidrug resistance proteins by a "two-faced transmembrane helix
    • Rath A., Melnyk R.A., and Deber C.M. Evidence for assembly of small multidrug resistance proteins by a "two-faced transmembrane helix. J. Biol. Chem. 281 (2006) 15546-15553
    • (2006) J. Biol. Chem. , vol.281 , pp. 15546-15553
    • Rath, A.1    Melnyk, R.A.2    Deber, C.M.3
  • 32
    • 20944444557 scopus 로고    scopus 로고
    • Computational analysis of membrane proteins: genomic occurrence, structure prediction and helix interactions
    • Lehnert U., et al. Computational analysis of membrane proteins: genomic occurrence, structure prediction and helix interactions. Q. Rev. Biophys. 37 (2004) 121-146
    • (2004) Q. Rev. Biophys. , vol.37 , pp. 121-146
    • Lehnert, U.1
  • 33
    • 21744454309 scopus 로고    scopus 로고
    • Transmembrane helix prediction: a comparative evaluation and analysis
    • Cuthbertson J.M., Doyle D.A., and Sansom M.S. Transmembrane helix prediction: a comparative evaluation and analysis. Protein Eng. Des. Sel. 18 (2005) 295-308
    • (2005) Protein Eng. Des. Sel. , vol.18 , pp. 295-308
    • Cuthbertson, J.M.1    Doyle, D.A.2    Sansom, M.S.3
  • 34
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 35
    • 17844369968 scopus 로고    scopus 로고
    • Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae
    • Murata T., Yamato I., Kakinuma Y., Leslie A.G., and Walker J.E. Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae. Science 308 (2005) 654-659
    • (2005) Science , vol.308 , pp. 654-659
    • Murata, T.1    Yamato, I.2    Kakinuma, Y.3    Leslie, A.G.4    Walker, J.E.5
  • 36
    • 17844367330 scopus 로고    scopus 로고
    • Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus
    • Meier T., Polzer P., Diederichs K., Welte W., and Dimroth P. Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus. Science 308 (2005) 659-662
    • (2005) Science , vol.308 , pp. 659-662
    • Meier, T.1    Polzer, P.2    Diederichs, K.3    Welte, W.4    Dimroth, P.5
  • 37
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: structure and implications
    • MacKenzie K.R., Prestegard J.H., and Engelman D.M. A transmembrane helix dimer: structure and implications. Science 276 (1997) 131-133
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 38
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism
    • Locher K.P., Lee A.T., and Rees D.C. The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science 296 (2002) 1091-1098
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 39
    • 0037418859 scopus 로고    scopus 로고
    • Gating the selectivity filter in ClC chloride channels
    • Dutzler R., Campbell E.B., and MacKinnon R. Gating the selectivity filter in ClC chloride channels. Science 300 (2003) 108-112
    • (2003) Science , vol.300 , pp. 108-112
    • Dutzler, R.1    Campbell, E.B.2    MacKinnon, R.3
  • 40
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson R.J., and Locher K.P. Structure of a bacterial multidrug ABC transporter. Nature 443 (2006) 180-185
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 41
    • 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., and 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
  • 42
    • 2242431668 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel
    • Bass R.B., Strop P., Barclay M., and Rees D.C. Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel. Science 298 (2002) 1582-1587
    • (2002) Science , vol.298 , pp. 1582-1587
    • Bass, R.B.1    Strop, P.2    Barclay, M.3    Rees, D.C.4
  • 43
    • 33645748904 scopus 로고    scopus 로고
    • 2+ transporter
    • 2+ transporter. Nature 440 (2006) 833-837
    • (2006) Nature , vol.440 , pp. 833-837
    • Lunin, V.V.1
  • 44
    • 0031926765 scopus 로고    scopus 로고
    • Guidelines for membrane protein engineering derived from de novo designed model peptides
    • Liu L.P., and Deber C.M. Guidelines for membrane protein engineering derived from de novo designed model peptides. Biopolymers 47 (1998) 41-62
    • (1998) Biopolymers , vol.47 , pp. 41-62
    • Liu, L.P.1    Deber, C.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.