메뉴 건너뛰기




Volumn 397, Issue 1, 2010, Pages 179-189

Structure of the Membrane Domain of Human Erythrocyte Anion Exchanger 1 Revealed by Electron Crystallography

Author keywords

AE1; band 3; ClC transporter; cryo electron microscopy; two dimensional crystal

Indexed keywords

ANTIPORTER; DIMER; HUMAN ERYTHROCYTE ANION EXCHANGER 1; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 77249153631     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.01.027     Document Type: Article
Times cited : (38)

References (65)
  • 1
    • 0015236352 scopus 로고
    • Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane
    • Fairbanks G., Steck T.L., and Wallach D.F. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 10 (1971) 2606-2617
    • (1971) Biochemistry , vol.10 , pp. 2606-2617
    • Fairbanks, G.1    Steck, T.L.2    Wallach, D.F.3
  • 2
    • 0037470168 scopus 로고    scopus 로고
    • Identification of a critical ankyrin-binding loop on the cytoplasmic domain of erythrocyte membrane band 3 by crystal structure analysis and site-directed mutagenesis
    • Chang S.H., and Low P.S. Identification of a critical ankyrin-binding loop on the cytoplasmic domain of erythrocyte membrane band 3 by crystal structure analysis and site-directed mutagenesis. J. Biol. Chem. 278 (2003) 6879-6884
    • (2003) J. Biol. Chem. , vol.278 , pp. 6879-6884
    • Chang, S.H.1    Low, P.S.2
  • 3
    • 0021940465 scopus 로고
    • Interactions between protein 4.1 and band 3. An alternative binding site for an element of the membrane skeleton
    • Pasternack G.R., Anderson R.A., Leto T.L., and Marchesi V.T. Interactions between protein 4.1 and band 3. An alternative binding site for an element of the membrane skeleton. J. Biol. Chem. 260 (1985) 3676-3683
    • (1985) J. Biol. Chem. , vol.260 , pp. 3676-3683
    • Pasternack, G.R.1    Anderson, R.A.2    Leto, T.L.3    Marchesi, V.T.4
  • 4
    • 0029822180 scopus 로고    scopus 로고
    • Increased rotational mobility and extractability of band 3 from protein 4.2-deficient erythrocyte membranes: evidence of a role for protein 4.2 in strengthening the band 3-cytoskeleton linkage
    • Rybicki A.C., Schwartz R.S., Hustedt E.J., and Cobb C.E. Increased rotational mobility and extractability of band 3 from protein 4.2-deficient erythrocyte membranes: evidence of a role for protein 4.2 in strengthening the band 3-cytoskeleton linkage. Blood 88 (1996) 2745-2753
    • (1996) Blood , vol.88 , pp. 2745-2753
    • Rybicki, A.C.1    Schwartz, R.S.2    Hustedt, E.J.3    Cobb, C.E.4
  • 5
    • 0034329189 scopus 로고    scopus 로고
    • Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3
    • Zhang D., Kiyatkin A., Bolin J.T., and Low P.S. Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3. Blood 96 (2000) 2925-2933
    • (2000) Blood , vol.96 , pp. 2925-2933
    • Zhang, D.1    Kiyatkin, A.2    Bolin, J.T.3    Low, P.S.4
  • 7
    • 0034512705 scopus 로고    scopus 로고
    • Red blood cell function and blood storage
    • Hamasaki N., and Yamamoto M. Red blood cell function and blood storage. Vox Sang. 79 (2000) 191-197
    • (2000) Vox Sang. , vol.79 , pp. 191-197
    • Hamasaki, N.1    Yamamoto, M.2
  • 10
    • 0022615649 scopus 로고
    • Molecular aspects of band 3 protein-mediated anion transport across the red blood cell membrane
    • Passow H. Molecular aspects of band 3 protein-mediated anion transport across the red blood cell membrane. Rev. Physiol., Biochem. Pharmacol. 103 (1986) 61-203
    • (1986) Rev. Physiol., Biochem. Pharmacol. , vol.103 , pp. 61-203
    • Passow, H.1
  • 11
    • 0021099508 scopus 로고
    • Affinity labeling of erythrocyte band 3 protein with pyridoxal 5-phosphate. Involvement of the 35,000-dalton fragment in anion transport
    • Nanri H., Hamasaki N., and Minakami S. Affinity labeling of erythrocyte band 3 protein with pyridoxal 5-phosphate. Involvement of the 35,000-dalton fragment in anion transport. J. Biol. Chem. 258 (1983) 5985-5989
    • (1983) J. Biol. Chem. , vol.258 , pp. 5985-5989
    • Nanri, H.1    Hamasaki, N.2    Minakami, S.3
  • 12
    • 0028302592 scopus 로고
    • Band 3, the anion exchanger of the erythrocyte membrane, is also a flippase
    • Ortwein R., Oslender-Kohnen A., and Deuticke B. Band 3, the anion exchanger of the erythrocyte membrane, is also a flippase. Biochim. Biophys. Acta 1191 (1994) 317-323
    • (1994) Biochim. Biophys. Acta , vol.1191 , pp. 317-323
    • Ortwein, R.1    Oslender-Kohnen, A.2    Deuticke, B.3
  • 13
    • 0025938224 scopus 로고
    • Analysis of the oligomeric state of band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography. Oligomeric stability and origin of heterogeneity
    • Casey J.R., and Reithmeier R.A. Analysis of the oligomeric state of band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography. Oligomeric stability and origin of heterogeneity. J. Biol. Chem. 266 (1991) 15726-15737
    • (1991) J. Biol. Chem. , vol.266 , pp. 15726-15737
    • Casey, J.R.1    Reithmeier, R.A.2
  • 15
    • 0036427425 scopus 로고    scopus 로고
    • Importance of detergent and phospholipid in the crystallization of the human erythrocyte anion-exchanger membrane domain
    • Lemieux M.J., Reithmeier R.A., and Wang D.N. Importance of detergent and phospholipid in the crystallization of the human erythrocyte anion-exchanger membrane domain. J. Struct. Biol. 137 (2002) 322-332
    • (2002) J. Struct. Biol. , vol.137 , pp. 322-332
    • Lemieux, M.J.1    Reithmeier, R.A.2    Wang, D.N.3
  • 16
    • 0032510959 scopus 로고    scopus 로고
    • Effect of band 3 subunit equilibrium on the kinetics and affinity of ankyrin binding to erythrocyte membrane vesicles
    • Van Dort H.M., Moriyama R., and Low P.S. Effect of band 3 subunit equilibrium on the kinetics and affinity of ankyrin binding to erythrocyte membrane vesicles. J. Biol. Chem. 273 (1998) 14819-14826
    • (1998) J. Biol. Chem. , vol.273 , pp. 14819-14826
    • Van Dort, H.M.1    Moriyama, R.2    Low, P.S.3
  • 17
    • 0036318471 scopus 로고    scopus 로고
    • Band 3 mutations, distal renal tubular acidosis, and Southeast Asian ovalocytosis
    • Wrong O., Bruce L.J., Unwin R.J., Toye A.M., and Tanner M.J. Band 3 mutations, distal renal tubular acidosis, and Southeast Asian ovalocytosis. Kidney Int. 62 (2002) 10-19
    • (2002) Kidney Int. , vol.62 , pp. 10-19
    • Wrong, O.1    Bruce, L.J.2    Unwin, R.J.3    Toye, A.M.4    Tanner, M.J.5
  • 18
    • 40449104048 scopus 로고    scopus 로고
    • Dominant-negative effect of Southeast Asian ovalocytosis anion exchanger 1 in compound heterozygous distal renal tubular acidosis
    • Kittanakom S., Cordat E., and Reithmeier R.A. Dominant-negative effect of Southeast Asian ovalocytosis anion exchanger 1 in compound heterozygous distal renal tubular acidosis. Biochem. J. 410 (2008) 271-281
    • (2008) Biochem. J. , vol.410 , pp. 271-281
    • Kittanakom, S.1    Cordat, E.2    Reithmeier, R.A.3
  • 19
    • 0017801444 scopus 로고
    • - transport site of human red blood cells by a kinetic analysis of the inhibitory effects of a chemical probe
    • - transport site of human red blood cells by a kinetic analysis of the inhibitory effects of a chemical probe. Biochim. Biophys. Acta 508 (1978) 357-363
    • (1978) Biochim. Biophys. Acta , vol.508 , pp. 357-363
    • Shami, Y.1    Rothstein, A.2    Knauf, P.A.3
  • 20
    • 0028006541 scopus 로고
    • 2DIDS (4,4′-diisothiocyanodihydrostilbene-2,2′-disulfonic acid) molecule
    • 2DIDS (4,4′-diisothiocyanodihydrostilbene-2,2′-disulfonic acid) molecule. J. Biol. Chem. 269 (1994) 1918-1926
    • (1994) J. Biol. Chem. , vol.269 , pp. 1918-1926
    • Okubo, K.1    Kang, D.2    Hamasaki, N.3    Jennings, M.L.4
  • 21
    • 0242507462 scopus 로고    scopus 로고
    • Histidine-834 of human erythrocyte band 3 has an essential role in the conformational changes that occur during the band 3-mediated anion exchange
    • Jin X.R., Abe Y., Li C.Y., and Hamasaki N. Histidine-834 of human erythrocyte band 3 has an essential role in the conformational changes that occur during the band 3-mediated anion exchange. Biochemistry 42 (2003) 12927-12932
    • (2003) Biochemistry , vol.42 , pp. 12927-12932
    • Jin, X.R.1    Abe, Y.2    Li, C.Y.3    Hamasaki, N.4
  • 22
    • 0024372289 scopus 로고
    • Conformational change of band 3 protein induced by diethyl pyrocarbonate modification in human erythrocyte ghosts
    • Izuhara K., Okubo K., and Hamasaki N. Conformational change of band 3 protein induced by diethyl pyrocarbonate modification in human erythrocyte ghosts. Biochemistry 28 (1989) 4725-4728
    • (1989) Biochemistry , vol.28 , pp. 4725-4728
    • Izuhara, K.1    Okubo, K.2    Hamasaki, N.3
  • 23
    • 0023035535 scopus 로고
    • Monoclonal antibodies against human erythrocyte band 3 protein. Localization of proteolytic cleavage sites and stilbenedisulfonate-binding lysine residues
    • Jennings M.L., Anderson M.P., and Monaghan R. Monoclonal antibodies against human erythrocyte band 3 protein. Localization of proteolytic cleavage sites and stilbenedisulfonate-binding lysine residues. J. Biol. Chem. 261 (1986) 9002-9010
    • (1986) J. Biol. Chem. , vol.261 , pp. 9002-9010
    • Jennings, M.L.1    Anderson, M.P.2    Monaghan, R.3
  • 24
    • 0024511767 scopus 로고
    • Monoclonal antibodies to the membrane domain of the human erythrocyte anion transport protein. Localization of the C-terminus of the protein to the cytoplasmic side of the red cell membrane and distribution of the protein in some human tissues
    • Wainwright S.D., Tanner M.J., Martin G.E., Yendle J.E., and Holmes C. Monoclonal antibodies to the membrane domain of the human erythrocyte anion transport protein. Localization of the C-terminus of the protein to the cytoplasmic side of the red cell membrane and distribution of the protein in some human tissues. Biochem. J. 258 (1989) 211-220
    • (1989) Biochem. J. , vol.258 , pp. 211-220
    • Wainwright, S.D.1    Tanner, M.J.2    Martin, G.E.3    Yendle, J.E.4    Holmes, C.5
  • 25
    • 0030860847 scopus 로고    scopus 로고
    • Proteolytic cleavage sites of band 3 protein in alkali-treated membranes: fidelity of hydropathy prediction for band 3 protein
    • Hamasaki N., Okubo K., Kuma H., Kang D., and Yae Y. Proteolytic cleavage sites of band 3 protein in alkali-treated membranes: fidelity of hydropathy prediction for band 3 protein. J. Biochem. 122 (1997) 577-585
    • (1997) J. Biochem. , vol.122 , pp. 577-585
    • Hamasaki, N.1    Okubo, K.2    Kuma, H.3    Kang, D.4    Yae, Y.5
  • 26
    • 3843064338 scopus 로고    scopus 로고
    • Mass spectrometric analyses of transmembrane proteins in human erythrocyte membrane
    • Abe Y., Chaen T., Jin X.R., Hamasaki T., and Hamasaki N. Mass spectrometric analyses of transmembrane proteins in human erythrocyte membrane. J. Biochem. 136 (2004) 97-106
    • (2004) J. Biochem. , vol.136 , pp. 97-106
    • Abe, Y.1    Chaen, T.2    Jin, X.R.3    Hamasaki, T.4    Hamasaki, N.5
  • 27
    • 0030745799 scopus 로고    scopus 로고
    • Mapping the ends of transmembrane segments in a polytopic membrane protein. Scanning N-glycosylation mutagenesis of extracytosolic loops in the anion exchanger, band 3
    • Popov M., Tam L.Y., Li J., and Reithmeier R.A. Mapping the ends of transmembrane segments in a polytopic membrane protein. Scanning N-glycosylation mutagenesis of extracytosolic loops in the anion exchanger, band 3. J. Biol. Chem. 272 (1997) 18325-18332
    • (1997) J. Biol. Chem. , vol.272 , pp. 18325-18332
    • Popov, M.1    Tam, L.Y.2    Li, J.3    Reithmeier, R.A.4
  • 28
    • 0033561328 scopus 로고    scopus 로고
    • Transmembrane folding of the human erythrocyte anion exchanger (AE1, band 3) determined by scanning and insertional N-glycosylation mutagenesis
    • Popov M., Li J., and Reithmeier R.A. Transmembrane folding of the human erythrocyte anion exchanger (AE1, band 3) determined by scanning and insertional N-glycosylation mutagenesis. Biochem. J. 339 (1999) 269-279
    • (1999) Biochem. J. , vol.339 , pp. 269-279
    • Popov, M.1    Li, J.2    Reithmeier, R.A.3
  • 29
    • 0037180396 scopus 로고    scopus 로고
    • The tenth membrane region of band 3 is initially exposed to the luminal side of the endoplasmic reticulum and then integrated into a partially folded band 3 intermediate
    • Kanki T., Sakaguchi M., Kitamura A., Sato T., Mihara K., and Hamasaki N. The tenth membrane region of band 3 is initially exposed to the luminal side of the endoplasmic reticulum and then integrated into a partially folded band 3 intermediate. Biochemistry 41 (2002) 13973-13981
    • (2002) Biochemistry , vol.41 , pp. 13973-13981
    • Kanki, T.1    Sakaguchi, M.2    Kitamura, A.3    Sato, T.4    Mihara, K.5    Hamasaki, N.6
  • 30
    • 0032575609 scopus 로고    scopus 로고
    • Topology of the region surrounding Glu681 of human AE1 protein, the erythrocyte anion exchanger
    • Tang X.B., Fujinaga J., Kopito R., and Casey J.R. Topology of the region surrounding Glu681 of human AE1 protein, the erythrocyte anion exchanger. J. Biol. Chem. 273 (1998) 22545-22553
    • (1998) J. Biol. Chem. , vol.273 , pp. 22545-22553
    • Tang, X.B.1    Fujinaga, J.2    Kopito, R.3    Casey, J.R.4
  • 31
    • 0033525686 scopus 로고    scopus 로고
    • Topology of the membrane domain of human erythrocyte anion exchange protein, AE1
    • Fujinaga J., Tang X.B., and Casey J.R. Topology of the membrane domain of human erythrocyte anion exchange protein, AE1. J. Biol. Chem. 274 (1999) 6626-6633
    • (1999) J. Biol. Chem. , vol.274 , pp. 6626-6633
    • Fujinaga, J.1    Tang, X.B.2    Casey, J.R.3
  • 32
    • 0037474222 scopus 로고    scopus 로고
    • Novel topology in C-terminal region of the human plasma membrane anion exchanger, AE1
    • Zhu Q., Lee D.W., and Casey J.R. Novel topology in C-terminal region of the human plasma membrane anion exchanger, AE1. J. Biol. Chem. 278 (2003) 3112-3120
    • (2003) J. Biol. Chem. , vol.278 , pp. 3112-3120
    • Zhu, Q.1    Lee, D.W.2    Casey, J.R.3
  • 33
    • 0032555375 scopus 로고    scopus 로고
    • Functional reassembly of the anion transport domain of human red cell band 3 (AE1) from multiple and non-complementary fragments
    • Groves J.D., Wang L., and Tanner M.J. Functional reassembly of the anion transport domain of human red cell band 3 (AE1) from multiple and non-complementary fragments. FEBS Lett. 433 (1998) 223-227
    • (1998) FEBS Lett. , vol.433 , pp. 223-227
    • Groves, J.D.1    Wang, L.2    Tanner, M.J.3
  • 34
    • 0033572646 scopus 로고    scopus 로고
    • Structural model for the organization of the transmembrane spans of the human red-cell anion exchanger (band 3; AE1)
    • Groves J.D., and Tanner M.J. Structural model for the organization of the transmembrane spans of the human red-cell anion exchanger (band 3; AE1). Biochem. J. 344 (1999) 699-711
    • (1999) Biochem. J. , vol.344 , pp. 699-711
    • Groves, J.D.1    Tanner, M.J.2
  • 35
    • 0032561457 scopus 로고    scopus 로고
    • Assessment of topogenic functions of anticipated transmembrane segments of human band 3
    • Ota K., Sakaguchi M., Hamasaki N., and Mihara K. Assessment of topogenic functions of anticipated transmembrane segments of human band 3. J. Biol. Chem. 273 (1998) 28286-28291
    • (1998) J. Biol. Chem. , vol.273 , pp. 28286-28291
    • Ota, K.1    Sakaguchi, M.2    Hamasaki, N.3    Mihara, K.4
  • 36
    • 0034703018 scopus 로고    scopus 로고
    • Membrane integration of the second transmembrane segment of band 3 requires a closely apposed preceding signal-anchor sequence
    • Ota K., Sakaguchi M., Hamasaki N., and Mihara K. Membrane integration of the second transmembrane segment of band 3 requires a closely apposed preceding signal-anchor sequence. J. Biol. Chem. 275 (2000) 29743-29748
    • (2000) J. Biol. Chem. , vol.275 , pp. 29743-29748
    • Ota, K.1    Sakaguchi, M.2    Hamasaki, N.3    Mihara, K.4
  • 37
    • 33750742309 scopus 로고    scopus 로고
    • Identification of oxidized methionine sites in erythrocyte membrane protein by liquid chromatography/electrospray ionization mass spectrometry peptide mapping
    • Li C., Takazaki S., Jin X., Kang D., Abe Y., and Hamasaki N. Identification of oxidized methionine sites in erythrocyte membrane protein by liquid chromatography/electrospray ionization mass spectrometry peptide mapping. Biochemistry 45 (2006) 12117-12124
    • (2006) Biochemistry , vol.45 , pp. 12117-12124
    • Li, C.1    Takazaki, S.2    Jin, X.3    Kang, D.4    Abe, Y.5    Hamasaki, N.6
  • 38
    • 0023203804 scopus 로고
    • Chemical modification and labeling of glutamate residues at the stilbenedisulfonate site of human red blood cell band 3 protein
    • Jennings M.L., and Anderson M.P. Chemical modification and labeling of glutamate residues at the stilbenedisulfonate site of human red blood cell band 3 protein. J. Biol. Chem. 262 (1987) 1691-1697
    • (1987) J. Biol. Chem. , vol.262 , pp. 1691-1697
    • Jennings, M.L.1    Anderson, M.P.2
  • 39
    • 0030024722 scopus 로고    scopus 로고
    • Topological disposition of tyrosine 486 in anion exchanger from human erythrocytes
    • Kalo M.S. Topological disposition of tyrosine 486 in anion exchanger from human erythrocytes. Biochemistry 35 (1996) 999-1009
    • (1996) Biochemistry , vol.35 , pp. 999-1009
    • Kalo, M.S.1
  • 40
    • 33745738625 scopus 로고    scopus 로고
    • The functional role of arginine 901 at the C-terminus of the human anion transporter band 3 protein
    • Takazaki S., Abe Y., Kang D., Li C., Jin X., Ueda T., and Hamasaki N. The functional role of arginine 901 at the C-terminus of the human anion transporter band 3 protein. J. Biochem. 139 (2006) 903-912
    • (2006) J. Biochem. , vol.139 , pp. 903-912
    • Takazaki, S.1    Abe, Y.2    Kang, D.3    Li, C.4    Jin, X.5    Ueda, T.6    Hamasaki, N.7
  • 41
    • 0037066082 scopus 로고    scopus 로고
    • Topology of the anion exchange protein AE1: the controversial sidedness of lysine 743
    • Kuma H., Shinde A.A., Howren T.R., and Jennings M.L. Topology of the anion exchange protein AE1: the controversial sidedness of lysine 743. Biochemistry 41 (2002) 3380-3388
    • (2002) Biochemistry , vol.41 , pp. 3380-3388
    • Kuma, H.1    Shinde, A.A.2    Howren, T.R.3    Jennings, M.L.4
  • 42
    • 0037066128 scopus 로고    scopus 로고
    • Molecular basis and functional consequences of the dominant effects of the mutant band 3 on the structure of normal band 3 in Southeast Asian ovalocytosis
    • Kuma H., Abe Y., Askin D., Bruce L.J., Hamasaki T., Tanner M.J., and Hamasaki N. Molecular basis and functional consequences of the dominant effects of the mutant band 3 on the structure of normal band 3 in Southeast Asian ovalocytosis. Biochemistry 41 (2002) 3311-3320
    • (2002) Biochemistry , vol.41 , pp. 3311-3320
    • Kuma, H.1    Abe, Y.2    Askin, D.3    Bruce, L.J.4    Hamasaki, T.5    Tanner, M.J.6    Hamasaki, N.7
  • 43
    • 0030888062 scopus 로고    scopus 로고
    • Complementation studies with co-expressed fragments of the human red cell anion transporter (band 3; AE1). The role of some exofacial loops in anion transport
    • Wang L., Groves J.D., Mawby W.J., and Tanner M.J. Complementation studies with co-expressed fragments of the human red cell anion transporter (band 3; AE1). The role of some exofacial loops in anion transport. J. Biol. Chem. 272 (1997) 10631-10638
    • (1997) J. Biol. Chem. , vol.272 , pp. 10631-10638
    • Wang, L.1    Groves, J.D.2    Mawby, W.J.3    Tanner, M.J.4
  • 44
    • 0030745799 scopus 로고    scopus 로고
    • Mapping the ends of transmembrane segments in a polytopic membrane protein
    • Popov M., Tam L.Y., Li J., and Reithmeier R.A. Mapping the ends of transmembrane segments in a polytopic membrane protein. J. Biol. Chem. 272 (1997) 18325-18332
    • (1997) J. Biol. Chem. , vol.272 , pp. 18325-18332
    • Popov, M.1    Tam, L.Y.2    Li, J.3    Reithmeier, R.A.4
  • 45
    • 0028339981 scopus 로고
    • Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, band 3
    • Wang D.N., Sarabia V.E., Reithmeier R.A., and Kühlbrandt W. Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, band 3. EMBO J. 13 (1994) 3230-3235
    • (1994) EMBO J. , vol.13 , pp. 3230-3235
    • Wang, D.N.1    Sarabia, V.E.2    Reithmeier, R.A.3    Kühlbrandt, W.4
  • 46
    • 76749162402 scopus 로고    scopus 로고
    • Helical image reconstruction of the outward-open human erythrocyte band 3 membrane domain in tubular crystals
    • 10.1016/j.jsb.2009.12.009
    • Yamaguchi T., Fujii T., Abe Y., Hirai T., Kang D., Namba K., et al. Helical image reconstruction of the outward-open human erythrocyte band 3 membrane domain in tubular crystals. J. Struct. Biol. (2009) 10.1016/j.jsb.2009.12.009
    • (2009) J. Struct. Biol.
    • Yamaguchi, T.1    Fujii, T.2    Abe, Y.3    Hirai, T.4    Kang, D.5    Namba, K.6
  • 48
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a ClC chloride channel at 3.0 Å 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 Å 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
  • 49
    • 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
  • 51
    • 0021180163 scopus 로고
    • Dimeric structure of single chloride channels from Torpedo electroplax
    • Miller C., and White M.M. Dimeric structure of single chloride channels from Torpedo electroplax. Proc. Natl Acad. Sci. USA 81 (1984) 2772-2775
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 2772-2775
    • Miller, C.1    White, M.M.2
  • 52
    • 0035843079 scopus 로고    scopus 로고
    • Projection structure of a ClC-type chloride channel at 6.5 Å resolution
    • Mindell J.A., Maduke M., Miller C., and Grigorieff N. Projection structure of a ClC-type chloride channel at 6.5 Å resolution. Nature 409 (2001) 219-223
    • (2001) Nature , vol.409 , pp. 219-223
    • Mindell, J.A.1    Maduke, M.2    Miller, C.3    Grigorieff, N.4
  • 53
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 55
    • 0035504871 scopus 로고    scopus 로고
    • Cysteine-directed cross-linking localizes regions of the human erythrocyte anion-exchange protein (AE1) relative to the dimeric interface
    • Taylor A.M., Zhu Q., and Casey J.R. Cysteine-directed cross-linking localizes regions of the human erythrocyte anion-exchange protein (AE1) relative to the dimeric interface. Biochem. J. 359 (2001) 661-668
    • (2001) Biochem. J. , vol.359 , pp. 661-668
    • Taylor, A.M.1    Zhu, Q.2    Casey, J.R.3
  • 56
    • 0028175436 scopus 로고
    • A method for alpha-helical integral membrane protein fold prediction
    • Taylor W.R., Jones D.T., and Green N.M. A method for alpha-helical integral membrane protein fold prediction. Proteins 18 (1994) 281-294
    • (1994) Proteins , vol.18 , pp. 281-294
    • Taylor, W.R.1    Jones, D.T.2    Green, N.M.3
  • 57
    • 0026760577 scopus 로고
    • A structural study of the membrane domain of band 3 by tryptic digestion. Conformational change of band 3 in situ induced by alkali treatment
    • Kang D., Okubo K., Hamasaki N., Kuroda N., and Shiraki H. A structural study of the membrane domain of band 3 by tryptic digestion. Conformational change of band 3 in situ induced by alkali treatment. J. Biol. Chem. 267 (1992) 19211-19217
    • (1992) J. Biol. Chem. , vol.267 , pp. 19211-19217
    • Kang, D.1    Okubo, K.2    Hamasaki, N.3    Kuroda, N.4    Shiraki, H.5
  • 58
    • 0032695274 scopus 로고    scopus 로고
    • Trehalose embedding technique for high-resolution electron crystallography: application to structural study on bacteriorhodopsin
    • Hirai T., Murata K., Mitsuoka K., Kimura Y., and Fujiyoshi Y. Trehalose embedding technique for high-resolution electron crystallography: application to structural study on bacteriorhodopsin. J. Electron Microsc. 48 (1999) 653-658
    • (1999) J. Electron Microsc. , vol.48 , pp. 653-658
    • Hirai, T.1    Murata, K.2    Mitsuoka, K.3    Kimura, Y.4    Fujiyoshi, Y.5
  • 59
    • 1942521362 scopus 로고    scopus 로고
    • Improved specimen preparation for cryo-electron microscopy using a symmetric carbon sandwich technique
    • Gyobu N., Tani K., Hiroaki Y., Kamegawa A., Mitsuoka K., and Fujiyoshi Y. Improved specimen preparation for cryo-electron microscopy using a symmetric carbon sandwich technique. J. Struct. Biol. 146 (2004) 325-333
    • (2004) J. Struct. Biol. , vol.146 , pp. 325-333
    • Gyobu, N.1    Tani, K.2    Hiroaki, Y.3    Kamegawa, A.4    Mitsuoka, K.5    Fujiyoshi, Y.6
  • 65
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.