메뉴 건너뛰기




Volumn 53, Issue 6, 1997, Pages 516-521

Three-dimensional structure of annexins

Author keywords

Annexin; Crystal structure; Electron microscopy; Interfacial membrane proteins; Ion channel

Indexed keywords

ANNEXIN; CALCIUM BINDING PROTEIN; ION CHANNEL; MEMBRANE PROTEIN; PHOSPHOLIPID BINDING PROTEIN;

EID: 0030821003     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050065     Document Type: Article
Times cited : (99)

References (51)
  • 1
    • 0023821674 scopus 로고
    • 2+-dependent phospholipid- (and membrane-) hinding proteins
    • 2+-dependent phospholipid- (and membrane-) hinding proteins. Biochemistry 27: 6645-6653
    • (1988) Biochemistry , vol.27 , pp. 6645-6653
    • Klee, C.B.1
  • 2
    • 0002179487 scopus 로고
    • Diversity in the annexin family
    • Heizmann, C. W. (ed.), Springer-Verlag, Berlin
    • Moss S. E., Edwards H. C. and Crumpton M. J. (1991) Diversity in the annexin family. In: Novel calcium-binding proteins, pp. 535-566, Heizmann, C. W. (ed.), Springer-Verlag, Berlin
    • (1991) Novel Calcium-binding Proteins , pp. 535-566
    • Moss, S.E.1    Edwards, H.C.2    Crumpton, M.J.3
  • 3
    • 0029644245 scopus 로고
    • Annexins: A novel family of calcium- and membrane-binding proteins in search of a function
    • Liemann S. and Lewit-Bentley A. (1995) Annexins: a novel family of calcium- and membrane-binding proteins in search of a function. Structure 3: 233-237
    • (1995) Structure , vol.3 , pp. 233-237
    • Liemann, S.1    Lewit-Bentley, A.2
  • 4
    • 0028324464 scopus 로고
    • Annexins: The problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins
    • Raynal P. and Pollard H. B. (1994) Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins. Biochim. Biophys. Acta 1197: 63-93
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 63-93
    • Raynal, P.1    Pollard, H.B.2
  • 5
    • 0028233432 scopus 로고
    • Annexin structure and membrane interactions: A molecular perspective
    • Swairjo M. A. and Seaton B. A. (1994a) Annexin structure and membrane interactions: a molecular perspective. Ann. Rev. Biophys. Biomolec. Struct. 23: 193-213
    • (1994) Ann. Rev. Biophys. Biomolec. Struct. , vol.23 , pp. 193-213
    • Swairjo, M.A.1    Seaton, B.A.2
  • 7
    • 0024535657 scopus 로고
    • Two lipocortin-like proteins, endonexin II and anchorin CII, may be alternate splices of the same gene
    • Haigler H. T., Fitch J. M., Jones J. M. and Schlaepfer D. D. (1989) Two lipocortin-like proteins, endonexin II and anchorin CII, may be alternate splices of the same gene. Trends Biochem. Sci. 14: 48-50
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 48-50
    • Haigler, H.T.1    Fitch, J.M.2    Jones, J.M.3    Schlaepfer, D.D.4
  • 8
    • 0028342872 scopus 로고
    • Structural evolution of the annexin supergene family
    • Smith P. D. and Moss S. E. (1994) Structural evolution of the annexin supergene family. Trends Genet. 10: 241-246
    • (1994) Trends Genet. , vol.10 , pp. 241-246
    • Smith, P.D.1    Moss, S.E.2
  • 10
    • 0023051747 scopus 로고
    • Consensus in exocytosis
    • Kretsinger R. H. and Creutz C. E. (1986) Consensus in exocytosis. Nature 302: 573
    • (1986) Nature , vol.302 , pp. 573
    • Kretsinger, R.H.1    Creutz, C.E.2
  • 11
    • 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. and Pâques E. P. (1990) The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes. EMBO J. 9: 3867-3874
    • (1990) EMBO J. , vol.9 , pp. 3867-3874
    • Huber, R.1    Römisch, J.2    Pâques, E.P.3
  • 12
    • 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. et al. (1992) 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. Molec. Biol. 223: 683-704
    • (1992) J. Molec. Biol. , vol.223 , pp. 683-704
    • Huber, R.1    Berendes, R.2    Burger, A.3    Schneider, M.4    Karshikov, A.5    Luecke, H.6
  • 13
    • 0026497557 scopus 로고
    • The effect of metal binding on the structure of annexin V and implications for membrane binding
    • Lewit-Bentley A., Morera S., Huber R. and Bodo G. (1992) The effect of metal binding on the structure of annexin V and implications for membrane binding. Eur. J. Biochem. 210: 73-77
    • (1992) Eur. J. Biochem. , vol.210 , pp. 73-77
    • Lewit-Bentley, A.1    Morera, S.2    Huber, R.3    Bodo, G.4
  • 14
    • 0027145153 scopus 로고
    • The crystal structure of a new high-calcium form of annexin V
    • Sopkova J., Renouard M. and Lewit-Bentley A. (1993) The crystal structure of a new high-calcium form of annexin V. J. Molec. Biol. 234: 816-825
    • (1993) J. Molec. Biol. , vol.234 , pp. 816-825
    • Sopkova, J.1    Renouard, M.2    Lewit-Bentley, A.3
  • 17
    • 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. and Russo-Marie F. (1996) The high-resolution crystal structure of human annexin III shows subtle differences with annexin V. Biochemistry 35: 1740-1744
    • (1996) Biochemistry , vol.35 , pp. 1740-1744
    • Favier-Perron, B.1    Lewit-Bentley, A.2    Russo-Marie, F.3
  • 18
    • 0030564834 scopus 로고    scopus 로고
    • The structure of recombinant human annexin VI in crystals and membrane-bound
    • Benz J., Bergner A., Hofmann A., Demange P., Göttig P., Liemann S. et al. (1996) The structure of recombinant human annexin VI in crystals and membrane-bound. J. Molec. Biol. 260: 638-643
    • (1996) J. Molec. Biol. , vol.260 , pp. 638-643
    • Benz, J.1    Bergner, A.2    Hofmann, A.3    Demange, P.4    Göttig, P.5    Liemann, S.6
  • 19
    • 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. and Haigler H. T. (1995) Crystal structure of the annexin XII hexamer and implications for bilayer insertion. Nature 378: 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
  • 21
    • 0029887641 scopus 로고    scopus 로고
    • The crystal structure and ion channel activity of human annexin II, a peripheral membrane protein
    • Burger A., Berendes R., Liemann S., Benz J., Hofmann A., Göttig P. et al. (1996) The crystal structure and ion channel activity of human annexin II, a peripheral membrane protein. J. Molec. Biol. 257: 839-847
    • (1996) J. Molec. Biol. , vol.257 , pp. 839-847
    • Burger, A.1    Berendes, R.2    Liemann, S.3    Benz, J.4    Hofmann, A.5    Göttig, P.6
  • 22
    • 0022539982 scopus 로고
    • 2+ and lipid-binding proteins
    • 2+ and lipid-binding proteins. FEBS Lett. 203: 99-103
    • (1986) FEBS Lett. , vol.203 , pp. 99-103
    • Geisow, M.J.1
  • 23
    • 0028326894 scopus 로고
    • The dynamic behavior of annexin V as a function of calcium ion binding: A circular dichroism, UV absorption, and steady-state and time-resolved fluorescence study
    • Sopkova J., Gallay J., Vincent M., Pancoska P. and Lewit-Bentley A. (1994) The dynamic behavior of annexin V as a function of calcium ion binding: a circular dichroism, UV absorption, and steady-state and time-resolved fluorescence study. Biochemistry 33: 4490-4499
    • (1994) Biochemistry , vol.33 , pp. 4490-4499
    • Sopkova, J.1    Gallay, J.2    Vincent, M.3    Pancoska, P.4    Lewit-Bentley, A.5
  • 24
    • 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. and Berendes R. (1994) 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. Molec. Biol. 237: 479-499
    • (1994) J. Molec. 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
  • 25
    • 0027514827 scopus 로고
    • Structure-function analysis of the ion channel selectivity filter in human annexin V
    • Berendes R., Voges D., Demange P., Huber R. and Burger A. (1993) Structure-function analysis of the ion channel selectivity filter in human annexin V. Science 262: 427-430
    • (1993) Science , vol.262 , pp. 427-430
    • Berendes, R.1    Voges, D.2    Demange, P.3    Huber, R.4    Burger, A.5
  • 26
    • 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. et al. (1996) Structural and functional characterisation of the voltage sensor in the ion channel human annexin V. J. Molec. Biol. 258: 555-561
    • (1996) J. Molec. Biol. , vol.258 , pp. 555-561
    • Liemann, S.1    Benz, J.2    Burger, A.3    Voges, D.4    Hofmann, A.5    Huber, R.6
  • 27
    • 0026711047 scopus 로고
    • Calcium channel and membrane fusion activity of synexin and other members of the Annexin gene family
    • Pollard H. B., Guy H. R., Arispe N., de la Fuente M., Lee G., Rojas E. M. et al. (1992) Calcium channel and membrane fusion activity of synexin and other members of the Annexin gene family. Biophys. J. 62: 15-18
    • (1992) Biophys. J. , vol.62 , pp. 15-18
    • Pollard, H.B.1    Guy, H.R.2    Arispe, N.3    De La Fuente, M.4    Lee, G.5    Rojas, E.M.6
  • 29
    • 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. and Burns A. L. (1990) Calcium-activated endonexin II forms calcium channels across acidic phospholipid bilayer membranes. J. Biol. Chem. 265: 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
  • 30
    • 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 L. Römisch J. and Pâques E. P. (1990b) 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 Lett. 275: 15-21
    • (1990) FEBS Lett. , vol.275 , pp. 15-21
    • Huber, R.1    Schneider, M.2    Mayr, L.3    Römisch, J.4    Pâques, E.P.5
  • 31
    • 0016627986 scopus 로고
    • Troponin and parvalbumin calcium binding regions predicted in myosin light chain and T4 lysozyme
    • Tufty R. M. and Kretsinger R. H. (1975) Troponin and parvalbumin calcium binding regions predicted in myosin light chain and T4 lysozyme. Science 187: 167-169
    • (1975) Science , vol.187 , pp. 167-169
    • Tufty, R.M.1    Kretsinger, R.H.2
  • 34
    • 0025344383 scopus 로고
    • Location of tryptophans in membrane-bound annexins
    • Meers P. (1990) Location of tryptophans in membrane-bound annexins. Biochemistry 29: 3325-3330
    • (1990) Biochemistry , vol.29 , pp. 3325-3330
    • Meers, P.1
  • 35
    • 0027300005 scopus 로고
    • Relationship between annexin V tryptophan exposure, calcium, and phospholipid binding
    • Meers P. and Mealy T. (1993) Relationship between annexin V tryptophan exposure, calcium, and phospholipid binding. Biochemistry 32: 5411-5418
    • (1993) Biochemistry , vol.32 , pp. 5411-5418
    • Meers, P.1    Mealy, T.2
  • 36
    • 0026473135 scopus 로고
    • Annexin V forms calcium-dependent trimeric units on phospholipid vesicles
    • Concha N. O., Head J. F., Kaetzel M. A., Dedman J. R. and Seaton B. A. (1992) Annexin V forms calcium-dependent trimeric units on phospholipid vesicles. FEBS Lett. 314: 159-162
    • (1992) FEBS Lett. , vol.314 , pp. 159-162
    • Concha, N.O.1    Head, J.F.2    Kaetzel, M.A.3    Dedman, J.R.4    Seaton, B.A.5
  • 37
    • 0025882865 scopus 로고
    • Structure of soluble and membrane-bound human annexin V
    • Brisson A., Mosser G. and Huber R. (1991) Structure of soluble and membrane-bound human annexin V. J. Molec. Biol. 220: 199-203
    • (1991) J. Molec. Biol. , vol.220 , pp. 199-203
    • Brisson, A.1    Mosser, G.2    Huber, R.3
  • 38
    • 0026029142 scopus 로고
    • Sub-domain structure of lipid-bound annexin-V resolved by electron image analysis
    • Mosser G., Ravanat C., Freyssinet J. M. and Brisson A. (1991) Sub-domain structure of lipid-bound annexin-V resolved by electron image analysis. J. Molec. Biol. 217: 241-245
    • (1991) J. Molec. Biol. , vol.217 , pp. 241-245
    • Mosser, G.1    Ravanat, C.2    Freyssinet, J.M.3    Brisson, A.4
  • 39
    • 0026060724 scopus 로고
    • 2D crystal forms of annexin IV on lipid monolayers
    • Newman R. H., Leonard K. and Crumpton M. J. (1991) 2D crystal forms of annexin IV on lipid monolayers. FEBS Lett. 279: 21-24
    • (1991) FEBS Lett. , vol.279 , pp. 21-24
    • Newman, R.H.1    Leonard, K.2    Crumpton, M.J.3
  • 40
    • 0028631772 scopus 로고
    • Two-dimensional structure of membrane-bound annexin V at 8 Å resolution
    • Olofsson A., Mallouh V. and Brisson A. (1994) Two-dimensional structure of membrane-bound annexin V at 8 Å resolution. J. Struct. Biol. 113: 199-205
    • (1994) J. Struct. Biol. , vol.113 , pp. 199-205
    • Olofsson, A.1    Mallouh, V.2    Brisson, A.3
  • 41
    • 0028245914 scopus 로고
    • Three-dimensional structure of membrane-bound annexin V. A correlative electron microscopy-X-ray crystallography study
    • Voges D., Berendes R., Burger A., Demange P., Baumeister W. and Huber R. (1994) Three-dimensional structure of membrane-bound annexin V. A correlative electron microscopy-X-ray crystallography study. J. Molec. Biol. 238: 199-213
    • (1994) J. Molec. Biol. , vol.238 , pp. 199-213
    • Voges, D.1    Berendes, R.2    Burger, A.3    Demange, P.4    Baumeister, W.5    Huber, R.6
  • 42
    • 0026724098 scopus 로고
    • A model of the structure of human annexin VI bound to lipid monolayers
    • Driessen H. P., Newman R. H., Freemont P. S. and Crumpton M. J. (1992) A model of the structure of human annexin VI bound to lipid monolayers. FEBS Lett. 306: 75-79
    • (1992) FEBS Lett. , vol.306 , pp. 75-79
    • Driessen, H.P.1    Newman, R.H.2    Freemont, P.S.3    Crumpton, M.J.4
  • 45
    • 0026439385 scopus 로고
    • A neutron solution scattering study of the structure of annexin-V and its binding to lipid vesicles
    • Ravanat C., Torbet J. and Freyssinet J. M. (1992) A neutron solution scattering study of the structure of annexin-V and its binding to lipid vesicles. J. Molec. Biol. 226: 1271-1278
    • (1992) J. Molec. Biol. , vol.226 , pp. 1271-1278
    • Ravanat, C.1    Torbet, J.2    Freyssinet, J.M.3
  • 47
    • 0025995720 scopus 로고
    • 2+-dependent annexin self-association on membrane surfaces
    • 2+-dependent annexin self-association on membrane surfaces. Biochemistry 30: 9607-9615
    • (1991) Biochemistry , vol.30 , pp. 9607-9615
    • Zaks, W.J.1    Creutz, C.E.2
  • 50
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24: 946-950
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 51
    • 0031552605 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal tetrad repeat from synexin (annexin VII) of Dictyostelium discoideum
    • in press
    • Liemann S., Bringemeier I., Benz J., Göttig P., Hofmann A., Huber R. et al. (1997) Crystal structure of the C-terminal tetrad repeat from synexin (annexin VII) of Dictyostelium discoideum. J. Molec. Biol., in press
    • (1997) J. Molec. Biol.
    • Liemann, S.1    Bringemeier, I.2    Benz, J.3    Göttig, P.4    Hofmann, A.5    Huber, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.