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Volumn 17, Issue 7, 2011, Pages 505-511

Folding and assembly of TMD 6-related segments of DMT 1 in trifluoroethanol aqueous solution

Author keywords

Assembly; DMT1 TMD6; NMR; Structure

Indexed keywords

ALANINE; GLYCINE; HISTIDINE; ISOLEUCINE; LYSINE; METHIONINE; MUTANT PROTEIN; NATURAL RESISTANCE ASSOCIATED MACROPHAGE PROTEIN 2; VALINE;

EID: 79958785603     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1356     Document Type: Article
Times cited : (9)

References (43)
  • 1
    • 0028962892 scopus 로고
    • Identification and characterization of a second mouse Nramp gene
    • Gruenheid S, Cellier M, Vidal S, Gros P. Identification and characterization of a second mouse Nramp gene. Genomics 1995; 25: 514-525.
    • (1995) Genomics , vol.25 , pp. 514-525
    • Gruenheid, S.1    Cellier, M.2    Vidal, S.3    Gros, P.4
  • 2
    • 0037126002 scopus 로고    scopus 로고
    • Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: implications for regulation and cellular function
    • Hubert N, Hentze MW. Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: implications for regulation and cellular function. Proc. Natl. Acad. Sci. U.S.A. 2002; 99: 12345-12350.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 12345-12350
    • Hubert, N.1    Hentze, M.W.2
  • 4
    • 13644278965 scopus 로고    scopus 로고
    • Age-dependent and iron-independent expression of two mRNA isoforms of divalent metal transporter 1 in rat brain
    • Ke Y, Chang YZ, Duan XL, Du JR, Zhu L, Wang K, Yang XD, Ho KP, Qian ZM. Age-dependent and iron-independent expression of two mRNA isoforms of divalent metal transporter 1 in rat brain. Neurobiol. Aging 2005; 26: 739-748.
    • (2005) Neurobiol. Aging , vol.26 , pp. 739-748
    • Ke, Y.1    Chang, Y.Z.2    Duan, X.L.3    Du, J.R.4    Zhu, L.5    Wang, K.6    Yang, X.D.7    Ho, K.P.8    Qian, Z.M.9
  • 5
    • 28444482404 scopus 로고    scopus 로고
    • Functional consequences of the human DMT1 (SLC11A2) mutation on protein expression and iron uptake
    • Priwitzerova M, Nie G, Sheftel AD, Pospisilova D, Divoky V, Ponka P. Functional consequences of the human DMT1 (SLC11A2) mutation on protein expression and iron uptake. Blood 2005; 106: 3985-3987.
    • (2005) Blood , vol.106 , pp. 3985-3987
    • Priwitzerova, M.1    Nie, G.2    Sheftel, A.D.3    Pospisilova, D.4    Divoky, V.5    Ponka, P.6
  • 6
    • 0033962110 scopus 로고    scopus 로고
    • Genetic susceptibility to intracellular infections: Nramp1, macrophage function and divalent cations transport
    • Gruenheid S, Gros P. Genetic susceptibility to intracellular infections: Nramp1, macrophage function and divalent cations transport. Curr. Opin. Microbiol. 2000; 3: 43-48.
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 43-48
    • Gruenheid, S.1    Gros, P.2
  • 7
    • 18244399587 scopus 로고    scopus 로고
    • Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver
    • Gunshin H, Fujiwara Y, Custodio AO, Direnzo C, Robine S, Andrews NC. Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver. J. Clin. Invest. 2005; 115: 1258-1266.
    • (2005) J. Clin. Invest. , vol.115 , pp. 1258-1266
    • Gunshin, H.1    Fujiwara, Y.2    Custodio, A.O.3    Direnzo, C.4    Robine, S.5    Andrews, N.C.6
  • 8
    • 0035865527 scopus 로고    scopus 로고
    • Expression of the DMT1 (NRAMP2/DCT1) iron transporter in mice with genetic iron overload disorders
    • Canonne-Hergaux F, Levy JE, Fleming MD, Montross LK, Andrews NC, Gros P. Expression of the DMT1 (NRAMP2/DCT1) iron transporter in mice with genetic iron overload disorders. Blood 2001; 97: 1138-1140.
    • (2001) Blood , vol.97 , pp. 1138-1140
    • Canonne-Hergaux, F.1    Levy, J.E.2    Fleming, M.D.3    Montross, L.K.4    Andrews, N.C.5    Gros, P.6
  • 10
    • 0041940266 scopus 로고    scopus 로고
    • Iron, manganese, and cobalt transport by Nramp1 (Slc11a1) and Nramp2 (Slc11a2) expressed at the plasma membrane
    • Forbes JR, Gros P. Iron, manganese, and cobalt transport by Nramp1 (Slc11a1) and Nramp2 (Slc11a2) expressed at the plasma membrane. Blood 2003; 102: 1884-1892.
    • (2003) Blood , vol.102 , pp. 1884-1892
    • Forbes, J.R.1    Gros, P.2
  • 11
    • 33746890568 scopus 로고    scopus 로고
    • The NRAMP family of metal-ion transporters
    • Nevo Y, Nelson N. The NRAMP family of metal-ion transporters. Biochim. Biophys. Acta 2006; 1763: 609-620.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 609-620
    • Nevo, Y.1    Nelson, N.2
  • 13
    • 0033575729 scopus 로고    scopus 로고
    • Metal-ion transporters and homeostasis
    • Nelson N. Metal-ion transporters and homeostasis. EMBO J. 1999; 18: 4361-4371.
    • (1999) EMBO J. , vol.18 , pp. 4361-4371
    • Nelson, N.1
  • 14
    • 0031794474 scopus 로고    scopus 로고
    • Sequence analyses and phylogenetic characterization of the ZIP family of metal ion transport proteins
    • Eng BH, Guerinot ML, Eide D, Saier MH Jr. Sequence analyses and phylogenetic characterization of the ZIP family of metal ion transport proteins. J. Membr. Biol. 1998; 166: 1-7.
    • (1998) J. Membr. Biol. , vol.166 , pp. 1-7
    • Eng, B.H.1    Guerinot, M.L.2    Eide, D.3    Saier Jr, M.H.4
  • 15
    • 0029155295 scopus 로고
    • Roles of histidine 752 and glutamate 699 in the pH dependence of mouse band 3 protein-mediated anion transport
    • Müller-Berger S, Karbach D, Kang D, Aranibar N, Wood PG, Rüterjans H, Passow H. Roles of histidine 752 and glutamate 699 in the pH dependence of mouse band 3 protein-mediated anion transport. Biochemistry 1995; 34: 9325-9332.
    • (1995) Biochemistry , vol.34 , pp. 9325-9332
    • Müller-Berger, S.1    Karbach, D.2    Kang, D.3    Aranibar, N.4    Wood, P.G.5    Rüterjans, H.6    Passow, H.7
  • 16
    • 33947400266 scopus 로고    scopus 로고
    • Recent progress in structure-function analyses of Nramp proton-dependent metal-ion transporters
    • Courville P, Chaloupka R, Cellier MF. Recent progress in structure-function analyses of Nramp proton-dependent metal-ion transporters. Biochem. Cell Biol. 2006; 84: 960-978.
    • (2006) Biochem. Cell Biol. , vol.84 , pp. 960-978
    • Courville, P.1    Chaloupka, R.2    Cellier, M.F.3
  • 17
    • 0037528706 scopus 로고    scopus 로고
    • Iron transport by Nramp2/DMT1: pH regulation of transport by 2 histidines in transmembrane domain 6
    • Lam-Yuk-Tseung S, Govoni G, Forbes J, Gros P. Iron transport by Nramp2/DMT1: pH regulation of transport by 2 histidines in transmembrane domain 6. Blood 2003; 101: 3699-3707.
    • (2003) Blood , vol.101 , pp. 3699-3707
    • Lam-Yuk-Tseung, S.1    Govoni, G.2    Forbes, J.3    Gros, P.4
  • 18
    • 77953713841 scopus 로고    scopus 로고
    • Identification of an "α-helix-extended segment-α-helix" conformation of the sixth transmembrane domain in DMT1
    • Xiao S, Li J, Wang Y, Wang C, Xue R, Wang S, Li F. Identification of an "α-helix-extended segment-α-helix" conformation of the sixth transmembrane domain in DMT1. Biochim. Biophys. Acta 2010; 1798: 1556-1564.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1556-1564
    • Xiao, S.1    Li, J.2    Wang, Y.3    Wang, C.4    Xue, R.5    Wang, S.6    Li, F.7
  • 19
    • 0024411870 scopus 로고
    • Protein measurement using bicinchoninic acid: elimination of interfering substances
    • Brown RE, Jarvis KL, Hyland KJ. Protein measurement using bicinchoninic acid: elimination of interfering substances. Anal. Biochem. 1989; 180: 136-139.
    • (1989) Anal. Biochem. , vol.180 , pp. 136-139
    • Brown, R.E.1    Jarvis, K.L.2    Hyland, K.J.3
  • 21
    • 79958823436 scopus 로고    scopus 로고
    • SPARKY 3, University of California, San Francisco.
    • Goddard TD, Kneller DG. SPARKY 3, University of California, San Francisco.
    • Goddard, T.D.1    Kneller, D.G.2
  • 22
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert P, Mumenthaler C, Wüthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 1997; 273: 283-298.
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 23
    • 0029633186 scopus 로고
    • AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules
    • Pearlman DA, Case DA, Caldwell JW, Ross WS, Cheatham TE III, DeBolt S, Ferguson D, Seibel G, Kollman P. AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules. Comput. Phys. Commun. 1995; 91: 1-41.
    • (1995) Comput. Phys. Commun. , vol.91 , pp. 1-41
    • Pearlman, D.A.1    Case, D.A.2    Caldwell, J.W.3    Ross, W.S.4    Cheatham III, T.E.5    DeBolt, S.6    Ferguson, D.7    Seibel, G.8    Kollman, P.9
  • 25
    • 20644449471 scopus 로고    scopus 로고
    • Modification of the generalized Born model suitable for macromolecules
    • Onufriev A, Bashford D, Case DA. Modification of the generalized Born model suitable for macromolecules. J. Phys. Chem. B 2000; 104: 3712-3720.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 3712-3720
    • Onufriev, A.1    Bashford, D.2    Case, D.A.3
  • 27
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 1996; 14: 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 28
    • 77951118565 scopus 로고    scopus 로고
    • Study on structure and assembly of the third transmembrane domain of Slc11a1
    • Xiao S, Wang Y, Yang L, Qi H, Wang C, Li F. Study on structure and assembly of the third transmembrane domain of Slc11a1. J. Pept. Sci. 2010; 16: 249-255.
    • (2010) J. Pept. Sci. , vol.16 , pp. 249-255
    • Xiao, S.1    Wang, Y.2    Yang, L.3    Qi, H.4    Wang, C.5    Li, F.6
  • 29
    • 0037014684 scopus 로고    scopus 로고
    • Solvation phenomena of a tetrapeptide in water/trifluoroethanol and water/ethanol mixtures: a diffusion NMR, intermolecular NOE, and molecular dynamics study
    • Fioroni M, Diaz MD, Burger K, Berger S. Solvation phenomena of a tetrapeptide in water/trifluoroethanol and water/ethanol mixtures: a diffusion NMR, intermolecular NOE, and molecular dynamics study. J. Am. Chem. Soc. 2002; 124: 7737-7744.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 7737-7744
    • Fioroni, M.1    Diaz, M.D.2    Burger, K.3    Berger, S.4
  • 30
    • 34250027242 scopus 로고    scopus 로고
    • Thermodynamic properties of binary mixtures of 2,2,2-trifluoroethanol with water or alkanols at T = 298.15 K
    • Minamihonoki T, Ogawa H, Nomuraa H, Murakami S. Thermodynamic properties of binary mixtures of 2, 2, 2-trifluoroethanol with water or alkanols at T = 298.15 K. Thermochim. Acta 2007; 459: 80-86.
    • (2007) Thermochim. Acta , vol.459 , pp. 80-86
    • Minamihonoki, T.1    Ogawa, H.2    Nomuraa, H.3    Murakami, S.4
  • 31
    • 0023049766 scopus 로고
    • Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences
    • Perkins SJ. Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Eur. J. Biochem. 1986; 157: 169-180.
    • (1986) Eur. J. Biochem. , vol.157 , pp. 169-180
    • Perkins, S.J.1
  • 32
    • 0026597879 scopus 로고
    • The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart DS, Sykes BD, Richards FM. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 1992; 31: 1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 36
    • 34447637751 scopus 로고    scopus 로고
    • Discontinuous membrane helices in transport proteins and their correlation with function
    • Screpanti E, Hunte C. Discontinuous membrane helices in transport proteins and their correlation with function. J. Struct. Biol. 2007; 159: 261-267.
    • (2007) J. Struct. Biol. , vol.159 , pp. 261-267
    • Screpanti, E.1    Hunte, C.2
  • 37
    • 33645504750 scopus 로고    scopus 로고
    • NMR study of the tetrameric KcsA potassium channel in detergent micelles
    • Chill JH, Louis JM, Miller C, Bax A. NMR study of the tetrameric KcsA potassium channel in detergent micelles. Protein Sci. 2006; 15: 684-698.
    • (2006) Protein Sci. , vol.15 , pp. 684-698
    • Chill, J.H.1    Louis, J.M.2    Miller, C.3    Bax, A.4
  • 38
    • 54849405417 scopus 로고    scopus 로고
    • Self-assembly of a simple membrane protein: coarse-grained molecular dynamics simulations of the influenza M2 channel
    • Carpenter T, Bond PJ, Khalid S, Sansom MS. Self-assembly of a simple membrane protein: coarse-grained molecular dynamics simulations of the influenza M2 channel. Biophys. J. 2008; 95: 3790-3801.
    • (2008) Biophys. J. , vol.95 , pp. 3790-3801
    • Carpenter, T.1    Bond, P.J.2    Khalid, S.3    Sansom, M.S.4
  • 39
    • 11144235539 scopus 로고    scopus 로고
    • Eukaryotic CTR copper uptake transporters require two faces of the third transmembrane domain for helix packing, oligomerization, and function
    • Aller SG, Eng ET, De Feo CJ, Unger VM. Eukaryotic CTR copper uptake transporters require two faces of the third transmembrane domain for helix packing, oligomerization, and function. J. Biol. Chem. 2004; 279: 53435-53441.
    • (2004) J. Biol. Chem. , vol.279 , pp. 53435-53441
    • Aller, S.G.1    Eng, E.T.2    De Feo, C.J.3    Unger, V.M.4
  • 41
    • 0035830743 scopus 로고    scopus 로고
    • Solution structure of micelle-bound H5 peptide (427-452): a primary structure corresponding to the pore forming region of the voltage dependent potassium channel
    • Shindo K, Takahashi H, Shinozaki K, Kami K, Anzai K, Lee S, Aoyagi H, Kirino Y, Shimada I. Solution structure of micelle-bound H5 peptide (427-452): a primary structure corresponding to the pore forming region of the voltage dependent potassium channel. Biochim. Biophys. Acta 2001; 1545: 153-159.
    • (2001) Biochim. Biophys. Acta , vol.1545 , pp. 153-159
    • Shindo, K.1    Takahashi, H.2    Shinozaki, K.3    Kami, K.4    Anzai, K.5    Lee, S.6    Aoyagi, H.7    Kirino, Y.8    Shimada, I.9
  • 43
    • 77954643198 scopus 로고    scopus 로고
    • Ion channel activity of transmembrane segment 6 Escherichia coli proton-dependent manganese transporter
    • Nunuková V, Urbánková E, Jelokhani-Niaraki M, Chaloupka R. Ion channel activity of transmembrane segment 6 Escherichia coli proton-dependent manganese transporter. Biopolymers 2010; 93: 718-726.
    • (2010) Biopolymers , vol.93 , pp. 718-726
    • Nunuková, V.1    Urbánková, E.2    Jelokhani-Niaraki, M.3    Chaloupka, R.4


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