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Volumn 270, Issue 1, 1997, Pages 79-88

Crystal structure of the C-terminal tetrad repeat from synexin (Annexin VII) of Dictyostelium discoideum

Author keywords

Annexin; Crystal structure; Dictyostelium; Ion channel; NMR

Indexed keywords

CALCIUM BINDING PROTEIN; CALCIUM ION; ION CHANNEL; RECOMBINANT PROTEIN; SYNEXIN; TYROSINE;

EID: 0031552605     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1091     Document Type: Article
Times cited : (25)

References (71)
  • 2
    • 0027412196 scopus 로고
    • ALSCRIPT: Tool to format multiple sequence alignments
    • Barton G. C. ALSCRIPT: tool to format multiple sequence alignments. Protein Eng. 6:1993;37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.C.1
  • 3
    • 0025678441 scopus 로고
    • Protein-protein recognition via short amphiphilic helices; A mutational analysis of the binding site of annexin II for p11
    • Becker T., Weber K., Johnsson N. Protein-protein recognition via short amphiphilic helices; a mutational analysis of the binding site of annexin II for p11. EMBO J. 9:1990;4207-4213.
    • (1990) EMBO J. , vol.9 , pp. 4207-4213
    • Becker, T.1    Weber, K.2    Johnsson, N.3
  • 5
    • 0027514827 scopus 로고
    • Structure-function analysis of the ion channel selectivity filter in human annexin V
    • Berendes R., Voges D., Demange P., Huber R., Burger A. Structure-function analysis of the ion channel selectivity filter in human annexin V. Science. 262:1993;427-430.
    • (1993) Science , vol.262 , pp. 427-430
    • Berendes, R.1    Voges, D.2    Demange, P.3    Huber, R.4    Burger, A.5
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M. M. A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 84985733652 scopus 로고
    • 1H-NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH
    • 1H-NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH. Biopolymers. 18:1979;285-312.
    • (1979) Biopolymers , vol.18 , pp. 285-312
    • Bundi, A.1    Wüthrich, K.2
  • 9
    • 0027203361 scopus 로고
    • A rapid and efficient purification method for recombinant annexin V for biophysical studies
    • Burger A., Berendes R., Voges D., Huber R., Demange P. A rapid and efficient purification method for recombinant annexin V for biophysical studies. FEBS Letters. 329:1993;25-28.
    • (1993) FEBS Letters , vol.329 , pp. 25-28
    • Burger, A.1    Berendes, R.2    Voges, D.3    Huber, R.4    Demange, P.5
  • 10
    • 0028263779 scopus 로고
    • Structural and electrophysiological analysis of annexin V mutants. Mutagenesis of human annexin V, an in vitro voltage-gated calcium channel, provides information about the structural features of the ion pathway, the voltage sensor and the ion selectivity filter
    • Burger A., Voges D., Demange P., Perez C. R., Huber R., Berendes R. Structural and electrophysiological analysis of annexin V mutants. Mutagenesis of human annexin V, an in vitro voltage-gated calcium channel, provides information about the structural features of the ion pathway, the voltage sensor and the ion selectivity filter. J. Mol. Biol. 237:1994;479-499.
    • (1994) J. Mol. Biol. , vol.237 , pp. 479-499
    • Burger, A.1    Voges, D.2    Demange, P.3    Perez, C.R.4    Huber, R.5    Berendes, R.6
  • 13
    • 0028949752 scopus 로고
    • Effect of protein synthesis inhibitors on synexin levels and secretory response in bovine adrenal medullary chromaffin cells
    • Cardenas A. M., Kuijpers G. A. J., Pollard H. B. Effect of protein synthesis inhibitors on synexin levels and secretory response in bovine adrenal medullary chromaffin cells. Biochim. Biophys. Acta. 1234:1995;255-260.
    • (1995) Biochim. Biophys. Acta , vol.1234 , pp. 255-260
    • Cardenas, A.M.1    Kuijpers, G.A.J.2    Pollard, H.B.3
  • 14
    • 0019784783 scopus 로고
    • Cis -Unsaturated fatty acids induce the fusion of chromaffin granules aggregated by synexin
    • Creutz C. E. cis -Unsaturated fatty acids induce the fusion of chromaffin granules aggregated by synexin. J. Cell Biol. 91:1981;247-256.
    • (1981) J. Cell Biol. , vol.91 , pp. 247-256
    • Creutz, C.E.1
  • 15
    • 0026452240 scopus 로고
    • The annexins and exocytosis
    • Creutz C. E. The annexins and exocytosis. Science. 258:1992;924-931.
    • (1992) Science , vol.258 , pp. 924-931
    • Creutz, C.E.1
  • 16
    • 0018136108 scopus 로고
    • Identification and purification of an adrenal medullary protein (synexin) that causes calcium-dependent aggregation of isolated chromaffin granules
    • Creutz C. E., Pazoles C. J., Pollard H. B. Identification and purification of an adrenal medullary protein (synexin) that causes calcium-dependent aggregation of isolated chromaffin granules. J. Biol. Chem. 253:1978;2858-2866.
    • (1978) J. Biol. Chem. , vol.253 , pp. 2858-2866
    • Creutz, C.E.1    Pazoles, C.J.2    Pollard, H.B.3
  • 20
    • 0026080022 scopus 로고
    • Dictyostelium annexin VII (synexin) cDNA sequence and isolation of a gene disruption mutant
    • Döring V., Schleicher M., Noegel A. A. Dictyostelium annexin VII (synexin) cDNA sequence and isolation of a gene disruption mutant. J. Biol. Chem. 266:1991;17509-17515.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17509-17515
    • Döring, V.1    Schleicher, M.2    Noegel, A.A.3
  • 22
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh R. A., Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A. 47:1991;392-400.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 25
    • 0021338180 scopus 로고
    • Isolation of a calcium dependent 35-kilodalton substrate for the epidermal growth factor receptor/kinase from A-431 cells
    • Fava R. A., Cohen S. Isolation of a calcium dependent 35-kilodalton substrate for the epidermal growth factor receptor/kinase from A-431 cells. J. Biol. Chem. 259:1984;497-509.
    • (1984) J. Biol. Chem. , vol.259 , pp. 497-509
    • Fava, R.A.1    Cohen, S.2
  • 26
    • 0030047497 scopus 로고    scopus 로고
    • The high-resolution crystal structure of human annexin III shows subtle differences with annexin V
    • Favier-Perron B., Lewit-Bentley A., Russo-Marie F. The high-resolution crystal structure of human annexin III shows subtle differences with annexin V. Biochemistry. 35:1996;1740-1744.
    • (1996) Biochemistry , vol.35 , pp. 1740-1744
    • Favier-Perron, B.1    Lewit-Bentley, A.2    Russo-Marie, F.3
  • 29
    • 0025978599 scopus 로고
    • Identification of a homologue for annexin VII (synexin) in Dictyostelium discoideum
    • Gerke V. Identification of a homologue for annexin VII (synexin) in Dictyostelium discoideum. J. Biol. Chem. 266:1991;1697-1700.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1697-1700
    • Gerke, V.1
  • 30
    • 0021299594 scopus 로고
    • Identity of p36 phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders; Calcium-dependent binding to non-erythroid spectrin and F-actin
    • Gerke V., Weber K. Identity of p36 phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders; calcium-dependent binding to non-erythroid spectrin and F-actin. EMBO J. 3:1984;227-233.
    • (1984) EMBO J. , vol.3 , pp. 227-233
    • Gerke, V.1    Weber, K.2
  • 31
    • 0001171815 scopus 로고
    • Amino-terminal sequence of p36 and associated p11: Identification of the site of tyrosine phosphorylation and homology with S100
    • Glenney J. R., Tack B. F. Amino-terminal sequence of p36 and associated p11: identification of the site of tyrosine phosphorylation and homology with S100. Proc. Natl Acad. Sci. USA. 82:1985;7884-7888.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 7884-7888
    • Glenney, J.R.1    Tack, B.F.2
  • 32
    • 0026080729 scopus 로고
    • Sequence and expression of annexin VII of Dictyostelium discoideum
    • Greenwood M., Tsang A. Sequence and expression of annexin VII of Dictyostelium discoideum. Biochim. Biophys. Acta. 1088:1991;429-432.
    • (1991) Biochim. Biophys. Acta , vol.1088 , pp. 429-432
    • Greenwood, M.1    Tsang, A.2
  • 35
    • 0025000276 scopus 로고
    • The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes
    • Huber R., Römisch J., Paques E. P. The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes. EMBO J. 9:1990a;3867-3874.
    • (1990) EMBO J. , vol.9 , pp. 3867-3874
    • Huber, R.1    Römisch, J.2    Paques, E.P.3
  • 36
    • 0025038549 scopus 로고
    • The calcium binding sites in human annexin V by crystal structure analysis at 2.0 Å resolution. Implications for membrane binding and calcium channel activity
    • Huber R., Schneider M., Mayr I., Römisch J., Paques E. P. The calcium binding sites in human annexin V by crystal structure analysis at 2.0 Å resolution. Implications for membrane binding and calcium channel activity. FEBS Letters. 275:1990b;15-21.
    • (1990) FEBS Letters , vol.275 , pp. 15-21
    • Huber, R.1    Schneider, M.2    Mayr, I.3    Römisch, J.4    Paques, E.P.5
  • 37
    • 0026575572 scopus 로고
    • Crystal and molecular structure of human annexin V after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins
    • Huber R., Berendes R., Burger A., Schneider M., Karshikov A., Luecke H., Römisch J., Paques E. Crystal and molecular structure of human annexin V after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins. J. Mol. Biol. 223:1992;683-704.
    • (1992) J. Mol. Biol. , vol.223 , pp. 683-704
    • Huber, R.1    Berendes, R.2    Burger, A.3    Schneider, M.4    Karshikov, A.5    Luecke, H.6    Römisch, J.7    Paques, E.8
  • 38
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and location of errors in these models
    • Jones T. A., Zou J.-Y., Cowan S., Kjeldgaard M. Improved methods for building protein models in electron density maps and location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.3    Kjeldgaard, M.4
  • 39
    • 0028147882 scopus 로고
    • A role for annexin IV in epithelial cell function. Inhibition of calcium-activated chloride conductance
    • Kaetzel M. A., Chan H. C., Dubinsky W. P., Dedman J. R., Nelson D. J. A role for annexin IV in epithelial cell function. Inhibition of calcium-activated chloride conductance. J. Biol. Chem. 269:1994;5297-5302.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5297-5302
    • Kaetzel, M.A.1    Chan, H.C.2    Dubinsky, W.P.3    Dedman, J.R.4    Nelson, D.J.5
  • 42
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 43
    • 0018816959 scopus 로고
    • Structure and evolution of calcium-modulated proteins
    • Kretsinger R. H. Structure and evolution of calcium-modulated proteins. CRC Crit. Rev. Biochem. 8:1980;119-174.
    • (1980) CRC Crit. Rev. Biochem. , vol.8 , pp. 119-174
    • Kretsinger, R.H.1
  • 44
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R. A., McArthur M. W., Moss D. S., Thorton J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    McArthur, M.W.2    Moss, D.S.3    Thorton, J.M.4
  • 46
    • 0029644245 scopus 로고
    • Annexins: A novel family of calcium- and membrane-binding proteins in search of a function
    • Liemann S., Lewit-Bentley A. Annexins: a novel family of calcium- and membrane-binding proteins in search of a function. Structure. 3:1995;233-237.
    • (1995) Structure , vol.3 , pp. 233-237
    • Liemann, S.1    Lewit-Bentley, A.2
  • 47
    • 0029918683 scopus 로고    scopus 로고
    • Structural and functional characterisation of the voltage sensor in the ion channel human annexin V
    • Liemann S., Benz J., Burger A., Voges D., Hofmann A., Huber R., Göttig P. Structural and functional characterisation of the voltage sensor in the ion channel human annexin V. J. Mol. Biol. 258:1996;555-561.
    • (1996) J. Mol. Biol. , vol.258 , pp. 555-561
    • Liemann, S.1    Benz, J.2    Burger, A.3    Voges, D.4    Hofmann, A.5    Huber, R.6    Göttig, P.7
  • 48
    • 0028795566 scopus 로고
    • Stilbene disulfonic acids inhibit synexin-mediated membrane aggregation and fusion
    • Liu L., Chander A. Stilbene disulfonic acids inhibit synexin-mediated membrane aggregation and fusion. Biochim. Biophys. Acta. 1254:1995;274-282.
    • (1995) Biochim. Biophys. Acta , vol.1254 , pp. 274-282
    • Liu, L.1    Chander, A.2
  • 49
    • 0028846237 scopus 로고
    • Crystal structure of the annexin XII hexamer and implications for bilayer insertion
    • Luecke H., Chang B. T., Maillard W. S., Schlaepfer D. D., Haigler H. T. Crystal structure of the annexin XII hexamer and implications for bilayer insertion. Nature. 378:1995;512-515.
    • (1995) Nature , vol.378 , pp. 512-515
    • Luecke, H.1    Chang, B.T.2    Maillard, W.S.3    Schlaepfer, D.D.4    Haigler, H.T.5
  • 50
    • 0025270075 scopus 로고
    • Polyproline, β-turn helices. Novel secondary structures proposed for the tandem repeats within rhodopsin, synaptophysin, synexin, gliadin, RNA polymerase II, hordein, and gluten
    • Matsushima N., Creutz C. E., Kretsinger R. H. Polyproline, β-turn helices. Novel secondary structures proposed for the tandem repeats within rhodopsin, synaptophysin, synexin, gliadin, RNA polymerase II, hordein, and gluten. Proteins: Struct. Funct. Genet. 7:1990;125-155.
    • (1990) Proteins: Struct. Funct. Genet. , vol.7 , pp. 125-155
    • Matsushima, N.1    Creutz, C.E.2    Kretsinger, R.H.3
  • 51
    • 0014432781 scopus 로고
    • Solvent contents of protein crystals
    • Matthews B. W. Solvent contents of protein crystals. J. Mol. Biol. 33:1968;491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 52
    • 0023891509 scopus 로고
    • Synexin enhances the aggregation rate but not the fusion rate of liposomes
    • Meers P., Bentz J., Alford D., Nir S., Papahadjopoulos D., Hong K. Synexin enhances the aggregation rate but not the fusion rate of liposomes. Biochemistry. 27:1988;4430-4439.
    • (1988) Biochemistry , vol.27 , pp. 4430-4439
    • Meers, P.1    Bentz, J.2    Alford, D.3    Nir, S.4    Papahadjopoulos, D.5    Hong, K.6
  • 53
    • 0028820642 scopus 로고
    • Molecular phylogeny of annexins and identification of a primitive homologue in Giardia lamblia
    • Morgan R. O., Fernández M.-P. Molecular phylogeny of annexins and identification of a primitive homologue in Giardia lamblia. Mol. Biol. Evol. 12:1995;967-979.
    • (1995) Mol. Biol. Evol. , vol.12 , pp. 967-979
    • Morgan, R.O.1    Fernández, M.-P.2
  • 54
    • 0003988303 scopus 로고
    • London and Chapel Hill: Portland Press
    • Moss S. E. The Annexins. 1992;Portland Press, London and Chapel Hill.
    • (1992) The Annexins
    • Moss, S.E.1
  • 56
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163.
    • (1994) Acta Crystallog. Sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 57
    • 0000732609 scopus 로고
    • GRASP-graphical representation and analysis of surface properties
    • Nicholls A., Bharadwaj R., Honig B. GRASP-graphical representation and analysis of surface properties. Biophys. J. 64:1993;A166.
    • (1993) Biophys. J. , vol.64 , pp. 166
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3
  • 58
    • 0024007049 scopus 로고
    • 2+channels in phosphatidylserine bilayer membranes
    • 2+channels in phosphatidylserine bilayer membranes. Proc. Natl Acad. Sci. USA. 85:1988;2974-2978.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 2974-2978
    • Pollard, H.B.1    Rojas, E.2
  • 59
    • 0025160854 scopus 로고
    • Synexin (annexin VII): A cytosolic calcium-binding protein which promotes membrane fusion and forms calcium channels in artificial bilayer and natural membranes
    • Pollard H. B., Burns A. L., Rojas E. Synexin (annexin VII): a cytosolic calcium-binding protein which promotes membrane fusion and forms calcium channels in artificial bilayer and natural membranes. J. Membr. Biol. 117:1990;101-112.
    • (1990) J. Membr. Biol. , vol.117 , pp. 101-112
    • Pollard, H.B.1    Burns, A.L.2    Rojas, E.3
  • 60
    • 0028324464 scopus 로고
    • Annexins: The problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins
    • Raynal P., Pollard H. B. Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins. Biochim. Biophys. Acta. 1197:1994;63-93.
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 63-93
    • Raynal, P.1    Pollard, H.B.2
  • 61
    • 0023648069 scopus 로고
    • Membrane capacity measurements suggest a calcium-dependent insertion of synexin into phosphatidylserine bilayers
    • Rojas E., Pollard H. B. Membrane capacity measurements suggest a calcium-dependent insertion of synexin into phosphatidylserine bilayers. FEBS Letters. 217:1987;25-31.
    • (1987) FEBS Letters , vol.217 , pp. 25-31
    • Rojas, E.1    Pollard, H.B.2
  • 62
    • 0025635905 scopus 로고
    • Calcium-activated endonexin II forms calcium channels across acidic phospholipid bilayer membranes
    • Rojas E., Pollard H. B., Haigler H. T., Parra C, Burns A. L. Calcium-activated endonexin II forms calcium channels across acidic phospholipid bilayer membranes. J. Biol. Chem. 265:1990;21207-21215.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21207-21215
    • Rojas, E.1    Pollard, H.B.2    Haigler, H.T.3    Parra, C.4    Burns, A.L.5
  • 63
    • 0027145153 scopus 로고
    • The crystal structure of a new high-calcium form of annexin V
    • Sopkova J., Renouard M., Lewit-Bentley A. The crystal structure of a new high-calcium form of annexin V. J. Mol. Biol. 234:1993;816-825.
    • (1993) J. Mol. Biol. , vol.234 , pp. 816-825
    • Sopkova, J.1    Renouard, M.2    Lewit-Bentley, A.3
  • 64
    • 0022549762 scopus 로고
    • A fluorescence assay for monitoring and analyzing fusion of biological membrane vesicles in vitro
    • Stuzin A. A fluorescence assay for monitoring and analyzing fusion of biological membrane vesicles in vitro. FEBS Letters. 197:1986;274-280.
    • (1986) FEBS Letters , vol.197 , pp. 274-280
    • Stuzin, A.1
  • 65
    • 0002878518 scopus 로고
    • Expression using the T7 RNA polymerase
    • F.A. Ausubel, R. Brent, R.E. Kingsten, D.D. Moore, J.G. Seidman, J.A. Smith, & K. Struhl. New York: Green Publishing and Wiley Interscience
    • Tabor S. Expression using the T7 RNA polymerase. Ausubel F. A., Brent R., Kingsten R. E., Moore D. D., Seidman J. G., Smith J. A., Struhl K. Current Protocols in Molecular Biology. 1990;Green Publishing and Wiley Interscience, New York.
    • (1990) Current Protocols in Molecular Biology
    • Tabor, S.1
  • 70
    • 0025995720 scopus 로고
    • 2+-dependent annexin self-association on membrane surfaces
    • 2+-dependent annexin self-association on membrane surfaces. Biochemistry. 30:1991;9607-9615.
    • (1991) Biochemistry , vol.30 , pp. 9607-9615
    • Zaks, W.J.1    Creutz, C.E.2
  • 71
    • 0027396098 scopus 로고
    • Mouse synexin (annexin VII) polymorphisms and a phylogenetic comparison with other synexins
    • Zhang-Keck Z. Y., Burns A. L., Pollard H. B. Mouse synexin (annexin VII) polymorphisms and a phylogenetic comparison with other synexins. Biochem. J. 289:1993;735-741.
    • (1993) Biochem. J. , vol.289 , pp. 735-741
    • Zhang-Keck, Z.Y.1    Burns, A.L.2    Pollard, H.B.3


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