메뉴 건너뛰기




Volumn 13, Issue 1, 2013, Pages

An analysis of oligomerization interfaces in transmembrane proteins

Author keywords

Eppic; GPCR; Lipids; Membrane proteins; Protein structure; Protein protein interfaces

Indexed keywords

G PROTEIN COUPLED RECEPTOR; MEMBRANE LIPID; MEMBRANE PROTEIN; PROTEIN; SMOOTHENED PROTEIN;

EID: 84885495867     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-13-21     Document Type: Article
Times cited : (31)

References (62)
  • 1
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3A resolution
    • DOI 10.1038/318618a0
    • Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 Å resolution. Deisenhofer J, Epp O, Miki K, Huber R, Michel H, Nature 1985 318 618 624 (Pubitemid 16172409)
    • (1985) Nature , vol.318 , Issue.6047 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3
  • 2
    • 0035795721 scopus 로고    scopus 로고
    • Amino acid distributions in integral membrane protein structures
    • DOI 10.1016/S0005-2736(01)00299-1, PII S0005273601002991
    • Amino acid distributions in integral membrane protein structures. Ulmschneider MB, Sansom MS, Biochim Biophys Acta 2001 1512 1 14 (Pubitemid 32378779)
    • (2001) Biochimica et Biophysica Acta - Biomembranes , vol.1512 , Issue.1 , pp. 1-14
    • Ulmschneider, M.B.1    Sansom, M.S.P.2
  • 3
    • 79751537491 scopus 로고
    • Lipid-binding surfaces of membrane proteins: Evidence from evolutionary and structural analysis
    • Lipid-binding surfaces of membrane proteins: evidence from evolutionary and structural analysis. Adamian L, Naveed H, Liang J, Biochim Biophys Acta 1808 2011 1092 1102
    • (1808) Biochim Biophys Acta , vol.2011 , pp. 1092-1102
    • Adamian, L.1    Naveed, H.2    Liang, J.3
  • 4
    • 0035943429 scopus 로고    scopus 로고
    • Helix-helix packing and interfacial pairwise interactions of residues in membrane proteins
    • DOI 10.1006/jmbi.2001.4908
    • Helix-helix packing and interfacial pairwise interactions of residues in membrane proteins. Adamian L, Liang J, J Mol Biol 2001 311 891 907 (Pubitemid 32803743)
    • (2001) Journal of Molecular Biology , vol.311 , Issue.4 , pp. 891-907
    • Adamian, L.1    Liang, J.2
  • 5
    • 28444482763 scopus 로고    scopus 로고
    • Interstrand pairing patterns in β-barrel membrane proteins: The positive-outside rule, aromatic rescue, and strand registration prediction
    • DOI 10.1016/j.jmb.2005.09.094, PII S0022283605011654
    • Interstrand pairing patterns in beta-barrel membrane proteins: the positive-outside rule, aromatic rescue, and strand registration prediction. Jackups R, Liang J, J Mol Biol 2005 354 979 993 (Pubitemid 41735517)
    • (2005) Journal of Molecular Biology , vol.354 , Issue.4 , pp. 979-993
    • Jackups Jr., R.1    Liang, J.2
  • 7
    • 7044274626 scopus 로고    scopus 로고
    • Lipids in membrane protein structures
    • DOI 10.1016/j.bbamem.2004.06.012, PII S0005273604001567, Lipid-Protein Interactions
    • Lipids in membrane protein structures. Palsdottir H, Hunte C, Biochim Biophys Acta 2004 1666 2 18 (Pubitemid 39425195)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1666 , Issue.1-2 , pp. 2-18
    • Palsdottir, H.1    Hunte, C.2
  • 8
    • 84871616988 scopus 로고    scopus 로고
    • The role of lipids in defining membrane protein interactions: Insights from mass spectrometry
    • The role of lipids in defining membrane protein interactions: insights from mass spectrometry. Barrera NP, Zhou M, Robinson CV, Trends Cell Biol 2013 23 1 8
    • (2013) Trends Cell Biol , vol.23 , pp. 1-8
    • Barrera, N.P.1    Zhou, M.2    Robinson, C.V.3
  • 9
    • 77951905043 scopus 로고    scopus 로고
    • Determinants of specificity at the protein-lipid interface in membranes
    • Determinants of specificity at the protein-lipid interface in membranes. Ernst AM, Contreras FX, Brügger B, Wieland F, Febs Lett 2010 584 1713 1720
    • (2010) Febs Lett , vol.584 , pp. 1713-1720
    • Ernst, A.M.1    Contreras, F.X.2    Brügger, B.3    Wieland, F.4
  • 10
    • 50349098382 scopus 로고    scopus 로고
    • Molecular simulations of lipid-mediated protein-protein interactions
    • Molecular simulations of lipid-mediated protein-protein interactions. De Meyer FJ-M, Venturoli M, Smit B, Biophys J 2008 95 1851 1865
    • (2008) Biophys J , vol.95 , pp. 1851-1865
    • De Meyer, F.-M.1    Venturoli, M.2    Smit, B.3
  • 11
    • 0035384692 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer microscopy: A mini review
    • DOI 10.1117/1.1383063
    • Fluorescence resonance energy transfer microscopy: a mini review. Periasamy A, J Biomed Opt 2001 6 287 291 (Pubitemid 32863911)
    • (2001) Journal of Biomedical Optics , vol.6 , Issue.3 , pp. 287-291
    • Periasamy, A.1
  • 13
    • 0030575833 scopus 로고    scopus 로고
    • Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator
    • DOI 10.1006/jmbi.1996.0595
    • Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator. Langosch D, Brosig B, Kolmar H, Fritz HJ, J Mol Biol 1996 263 525 530 (Pubitemid 26382072)
    • (1996) Journal of Molecular Biology , vol.263 , Issue.4 , pp. 525-530
    • Langosch, D.1    Brosig, B.2    Kolmar, H.3    Fritz, H.-J.4
  • 20
    • 0343847471 scopus 로고
    • Monomeric and aggregated bacteriorhodopsin: Single-turnover proton transport stoichiometry and photochemistry
    • Monomeric and aggregated bacteriorhodopsin: single-turnover proton transport stoichiometry and photochemistry. Grzesiek S, Dencher NA, Proc Natl Acad Sci USA 1988 85 9509 9513
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 9509-9513
    • Grzesiek, S.1    Dencher, N.A.2
  • 21
    • 0036301007 scopus 로고    scopus 로고
    • Bicelle crystallization: A new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure
    • DOI 10.1006/jmbi.2001.5295
    • Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure. Faham S, Bowie JU, J Mol Biol 2002 316 1 6 (Pubitemid 34729261)
    • (2002) Journal of Molecular Biology , vol.316 , Issue.1 , pp. 1-6
    • Faham, S.1    Bowie, J.U.2
  • 23
    • 21844441860 scopus 로고    scopus 로고
    • Monomeric G-protein-coupled receptor as a functional unit
    • DOI 10.1021/bi050720o
    • Monomeric G-protein-coupled receptor as a functional unit. Chabre M, Le Maire M, Biochemistry 2005 44 9395 9403 (Pubitemid 40962038)
    • (2005) Biochemistry , vol.44 , Issue.27 , pp. 9395-9403
    • Chabre, M.1    Le Maire, M.2
  • 24
    • 10844255797 scopus 로고    scopus 로고
    • Oligomerization of G protein-coupled receptors: Past, present, and future
    • DOI 10.1021/bi047907k
    • Oligomerization of G protein-coupled receptors: past, present, and future. Park PS-H, Filipek S, Wells JW, Palczewski K, Biochemistry 2004 43 15643 15656 (Pubitemid 39665065)
    • (2004) Biochemistry , vol.43 , Issue.50 , pp. 15643-15656
    • Park, P.S.-H.1    Filipek, S.2    Wells, J.W.3    Palczewski, K.4
  • 28
    • 84876197291 scopus 로고    scopus 로고
    • Crystal structure of oligomeric β(1)-adrenergic G protein-coupled receptors in ligand-free basal state
    • Crystal structure of oligomeric β(1)-adrenergic G protein-coupled receptors in ligand-free basal state. Huang J, Chen S, Zhang JJ, Huang X-Y, Nat Struct Mol Biol 2013 20 419 425
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 419-425
    • Huang, J.1    Chen, S.2    Zhang, J.J.3    Huang, X.-Y.4
  • 31
    • 27544484570 scopus 로고    scopus 로고
    • Structural basis for lipid-mediated interactions between mitochondrial ADP/ATP carrier monomers
    • DOI 10.1016/j.febslet.2005.09.061, PII S0014579305011798
    • Structural basis for lipid-mediated interactions between mitochondrial ADP/ATP carrier monomers. Nury H, Dahout-Gonzalez C, Trézéguet V, Lauquin G, Brandolin G, Pebay-Peyroula E, Febs Lett 2005 579 6031 6036 (Pubitemid 41546242)
    • (2005) FEBS Letters , vol.579 , Issue.27 , pp. 6031-6036
    • Nury, H.1    Dahout-Gonzalez, C.2    Trezeguet, V.3    Lauquin, G.4    Brandolin, G.5    Pebay-Peyroula, E.6
  • 32
    • 77955781875 scopus 로고    scopus 로고
    • CRK: An evolutionary approach for distinguishing biologically relevant interfaces from crystal contacts
    • CRK: an evolutionary approach for distinguishing biologically relevant interfaces from crystal contacts. Schärer MA, Grütter MG, Capitani G, Proteins 2010 78 2707 2713
    • (2010) Proteins , vol.78 , pp. 2707-2713
    • Schärer, M.A.1    Grütter, M.G.2    Capitani, G.3
  • 33
    • 0141669302 scopus 로고    scopus 로고
    • Automatic inference of protein quaternary structure from crystals
    • Automatic inference of protein quaternary structure from crystals. Ponstingl H, Kabir T, Thornton JM, J Appl Crystallogr 2003 36 1116 1122
    • (2003) J Appl Crystallogr , vol.36 , pp. 1116-1122
    • Ponstingl, H.1    Kabir, T.2    Thornton, J.M.3
  • 35
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • DOI 10.1006/jmbi.1993.1648
    • Shape complementarity at protein/protein interfaces. Lawrence MC, Colman PM, J Mol Biol 1993 234 946 950 (Pubitemid 24027225)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.4 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 37
    • 0036226583 scopus 로고    scopus 로고
    • Comparison of helix interactions in membrane and soluble α-bundle proteins
    • Comparison of helix interactions in membrane and soluble alpha-bundle proteins. Eilers M, Patel AB, Liu W, Smith SO, Biophys J 2002 82 2720 2736 (Pubitemid 34441309)
    • (2002) Biophysical Journal , vol.82 , Issue.5 , pp. 2720-2736
    • Eilers, M.1    Patel, A.B.2    Liu, W.3    Smith, S.O.4
  • 39
    • 0030804610 scopus 로고    scopus 로고
    • Stoichiometry of lipid-protein interaction and integral membrane protein structure
    • DOI 10.1007/s002490050072
    • Stoichiometry of lipid-protein interaction and integral membrane protein structure. Marsh D, Eur Biophys J 1997 26 203 208 (Pubitemid 27405100)
    • (1997) European Biophysics Journal , vol.26 , Issue.2 , pp. 203-208
    • Marsh, D.1
  • 40
    • 22544467474 scopus 로고    scopus 로고
    • 1 complex: A new crystal structure reveals an altered intramolecular hydrogen-bonding pattern
    • DOI 10.1016/j.jmb.2005.05.053, PII S0022283605006078
    • Binding of the respiratory chain inhibitor antimycin to the mitochondrial bc1 complex: a new crystal structure reveals an altered intramolecular hydrogen-bonding pattern. Huang L-S, Cobessi D, Tung EY, Berry EA, J Mol Biol 2005 351 573 597 (Pubitemid 41021942)
    • (2005) Journal of Molecular Biology , vol.351 , Issue.3 , pp. 573-597
    • Huang, L.-S.1    Cobessi, D.2    Tung, E.Y.3    Berry, E.A.4
  • 41
    • 0019316912 scopus 로고
    • Molecular weight and hydrodynamic parameters of the adenosine 5'-diphosphate-adenosine 5'-triphosphate carrier in Triton X-100
    • Molecular weight and hydrodynamic parameters of the adenosine 5'-diphosphate-adenosine 5'-triphosphate carrier in Triton X-100. Hackenberg H, Klingenberg M, Biochemistry 1980 19 548 555
    • (1980) Biochemistry , vol.19 , pp. 548-555
    • Hackenberg, H.1    Klingenberg, M.2
  • 42
    • 0242497235 scopus 로고    scopus 로고
    • Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside
    • DOI 10.1038/nature02056
    • Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside. Pebay-Peyroula E, Dahout-Gonzalez C, Kahn R, Trézéguet V, Lauquin GJ-M, Brandolin G, Nature 2003 426 39 44 (Pubitemid 37432535)
    • (2003) Nature , vol.426 , Issue.6962 , pp. 39-44
    • Pebay-Peyroula, E.1    Dahout-Gonzalez, C.2    Kahn, R.3    Trezeguet, V.4    Lauquin, G.J.-M.5    Brandolin, G.6
  • 43
    • 0036971196 scopus 로고    scopus 로고
    • Crystallographic structure of the K intermediate of bacteriorhodopsin: Conservation of free energy after photoisomerization of the retinal
    • DOI 10.1016/S0022-2836(02)00681-2
    • Crystallographic structure of the K intermediate of bacteriorhodopsin: conservation of free energy after photoisomerization of the retinal. Schobert B, Cupp-Vickery J, Hornak V, Smith S, Lanyi J, J Mol Biol 2002 321 715 726 (Pubitemid 36124806)
    • (2002) Journal of Molecular Biology , vol.321 , Issue.4 , pp. 715-726
    • Schobert, B.1    Cupp-Vickery, J.2    Hornak, V.3    Smith, S.O.4    Lanyi, J.K.5
  • 44
    • 84873572846 scopus 로고    scopus 로고
    • Techniques, tools and best practices for ligand electron-density analysis and results from their application to deposited crystal structures
    • Techniques, tools and best practices for ligand electron-density analysis and results from their application to deposited crystal structures. Pozharski E, Weichenberger CX, Rupp B, Acta Crystallogr D 2013 69 150 167
    • (2013) Acta Crystallogr D , vol.69 , pp. 150-167
    • Pozharski, E.1    Weichenberger, C.X.2    Rupp, B.3
  • 45
    • 79953868376 scopus 로고    scopus 로고
    • Crystallizing membrane proteins in lipidic mesophases. A host lipid screen
    • Crystallizing membrane proteins in lipidic mesophases. A host lipid screen. Li D, Lee J, Caffrey M, Cryst Growth Des 2011 11 530 537
    • (2011) Cryst Growth des , vol.11 , pp. 530-537
    • Li, D.1    Lee, J.2    Caffrey, M.3
  • 47
    • 39149104024 scopus 로고    scopus 로고
    • GPCR monomers and oligomers: It takes all kinds
    • GPCR monomers and oligomers: it takes all kinds. Gurevich VV, Gurevich EV, Trends Neurosci 2008 31 74 81
    • (2008) Trends Neurosci , vol.31 , pp. 74-81
    • Gurevich, V.V.1    Gurevich, E.V.2
  • 48
    • 84863255255 scopus 로고    scopus 로고
    • Structure and ligand recognition of class C GPCRs
    • Structure and ligand recognition of class C GPCRs. Chun L, Zhang W, Liu J, Acta Pharm Sinic 2012 33 312 323
    • (2012) Acta Pharm Sinic , vol.33 , pp. 312-323
    • Chun, L.1    Zhang, W.2    Liu, J.3
  • 49
    • 0037474238 scopus 로고    scopus 로고
    • Ligand-independent dimerization of CXCR4, a principal HIV-1 coreceptor
    • DOI 10.1074/jbc.M210140200
    • Ligand-independent dimerization of CXCR4, a principal HIV-1 coreceptor. Babcock GJ, Farzan M, Sodroski J, J Biol Chem 2003 278 3378 3385 (Pubitemid 36801253)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.5 , pp. 3378-3385
    • Babcock, G.J.1    Farzan, M.2    Sodroski, J.3
  • 52
    • 0032169688 scopus 로고    scopus 로고
    • PQS: A protein quaternary structure file server
    • DOI 10.1016/S0968-0004(98)01253-5, PII S0968000498012535
    • PQS: a protein quaternary structure file server. Henrick K, Thornton JM, Trends Biochem Sci 1998 23 358 361 (Pubitemid 28461869)
    • (1998) Trends in Biochemical Sciences , vol.23 , Issue.9 , pp. 358-361
    • Henrick, K.1    Thornton, J.M.2
  • 53
    • 0035914476 scopus 로고    scopus 로고
    • Conservation Helps to Identify Biologically Relevant Crystal Contacts
    • DOI 10.1006/jmbi.2001.5034, PII S002228360195034X
    • Conservation helps to identify biologically relevant crystal contacts. Valdar WS, Thornton JM, J Mol Biol 2001 313 399 416 (Pubitemid 33587196)
    • (2001) Journal of Molecular Biology , vol.313 , Issue.2 , pp. 399-416
    • Valdar, W.S.J.1    Thornton, J.M.2
  • 54
    • 34548232365 scopus 로고    scopus 로고
    • Inference of Macromolecular Assemblies from Crystalline State
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Inference of macromolecular assemblies from crystalline state. Krissinel E, Henrick K, J Mol Biol 2007 372 774 797 (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 56
    • 36049033946 scopus 로고    scopus 로고
    • Hedgehog regulates smoothened activity by inducing a conformational switch
    • DOI 10.1038/nature06225, PII NATURE06225
    • Hedgehog regulates smoothened activity by inducing a conformational switch. Zhao Y, Tong C, Jiang J, Nature 2007 450 252 258 (Pubitemid 350100532)
    • (2007) Nature , vol.450 , Issue.7167 , pp. 252-258
    • Zhao, Y.1    Tong, C.2    Jiang, J.3
  • 58
    • 33644861214 scopus 로고    scopus 로고
    • OPM: Orientations of proteins in membranes database
    • DOI 10.1093/bioinformatics/btk023
    • OPM: orientations of proteins in membranes database. Lomize MA, Lomize AL, Pogozheva ID, Mosberg HI, Bioinformatics 2006 22 623 625 (Pubitemid 43372827)
    • (2006) Bioinformatics , vol.22 , Issue.5 , pp. 623-625
    • Lomize, M.A.1    Lomize, A.L.2    Pogozheva, I.D.3    Mosberg, H.I.4
  • 59
    • 10244252813 scopus 로고    scopus 로고
    • Transmembrane proteins in the Protein Data Bank: Identification and classification
    • DOI 10.1093/bioinformatics/bth340
    • Transmembrane proteins in the protein data bank: identification and classification. Tusnády GE, Dosztányi Z, Simon I, Bioinformatics 2004 20 2964 2972 (Pubitemid 39619188)
    • (2004) Bioinformatics , vol.20 , Issue.17 , pp. 2964-2972
    • Tusnady, G.E.1    Dosztanyi, Z.2    Simon, I.3
  • 60
    • 0002344794 scopus 로고
    • Bootstrap methods: Another look at the jackknife
    • Bootstrap methods: another look at the jackknife. Efron B, The annals of Statistics 1979 7 1 26
    • (1979) The Annals of Statistics , vol.7 , pp. 1-26
    • Efron, B.1
  • 61
    • 79951480123 scopus 로고    scopus 로고
    • R Development Core Team Vienna Austria: R Foundation for Statistical Computing
    • R Development Core Team, R: A Language and Environment for Statistical Computing Vienna Austria: R Foundation for Statistical Computing 2010
    • (2010) R: A Language and Environment for Statistical Computing


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.