메뉴 건너뛰기




Volumn 24, Issue 3, 2005, Pages 175-185

Theoretically predicted structures of plasma membrane Ca 2+-ATPase and their susceptibilities to oxidation

Author keywords

Calmodulin; Homology modeling; Molecular dynamics; Oxidation; Plasma membrane Ca2+ ATPase; PMCA; Threading

Indexed keywords

ADENOSINETRIPHOSPHATE; BRAIN; CALCIUM; DISEASES; ENZYME KINETICS; HYDROPHOBICITY; MEMBRANES; MOLECULAR DYNAMICS; OXIDATION;

EID: 27144434776     PISSN: 10933263     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmgm.2005.07.003     Document Type: Article
Times cited : (31)

References (59)
  • 1
    • 16544385106 scopus 로고    scopus 로고
    • The ambivalent nature of the calcium signal
    • E. Carafoli The ambivalent nature of the calcium signal J. Endocrinol. Invest. 27 2004 134 136
    • (2004) J. Endocrinol. Invest. , vol.27 , pp. 134-136
    • Carafoli, E.1
  • 2
    • 0034161430 scopus 로고    scopus 로고
    • Mechanisms of calcium decay kinetics in hippocampal spines: Role of spine calcium pumps and calcium diffusion through the spine neck in biochemical compartmentalization
    • A. Majewska, E. Brown, J. Ross, and R. Yuste Mechanisms of calcium decay kinetics in hippocampal spines: role of spine calcium pumps and calcium diffusion through the spine neck in biochemical compartmentalization J. Neurosci. 20 2000 1722 1734
    • (2000) J. Neurosci. , vol.20 , pp. 1722-1734
    • Majewska, A.1    Brown, E.2    Ross, J.3    Yuste, R.4
  • 3
    • 26044453852 scopus 로고    scopus 로고
    • Calcium signaling: A historical account
    • E. Carafoli Calcium signaling: a historical account Biol. Res. 37 2004 497 505
    • (2004) Biol. Res. , vol.37 , pp. 497-505
    • Carafoli, E.1
  • 4
    • 0025187798 scopus 로고
    • Structural and functional aspects of calcium homeostasis in eukaryotic cells
    • D. Pietrobon, F. Di Virgilio, and T. Pozzan Structural and functional aspects of calcium homeostasis in eukaryotic cells Eur. J. Biochem. 193 1990 599 622
    • (1990) Eur. J. Biochem. , vol.193 , pp. 599-622
    • Pietrobon, D.1    Di Virgilio, F.2    Pozzan, T.3
  • 5
    • 0024473312 scopus 로고
    • 2+-pumping ATPase of cardia sarcolemma in four states of activation
    • 2+-pumping ATPase of cardia sarcolemma in four states of activation J. Biol. Chem. 264 1989 13612 13622
    • (1989) J. Biol. Chem. , vol.264 , pp. 13612-13622
    • Dixon, D.A.1    Haynes, D.H.2
  • 7
    • 85047692204 scopus 로고
    • The plasma membrane calcium pump: Structure, function, regulation
    • E. Carafoli The plasma membrane calcium pump: structure, function, regulation Biochim. Biophys. Acta 1101 1992 266 267
    • (1992) Biochim. Biophys. Acta , vol.1101 , pp. 266-267
    • Carafoli, E.1
  • 8
    • 0031964372 scopus 로고    scopus 로고
    • Evolution of substrate specificities in the P-type ATPase superfamily
    • K.B. Axelsen, and M.G. Palmgren Evolution of substrate specificities in the P-type ATPase superfamily J. Mol. Evol. 46 1998 84 101
    • (1998) J. Mol. Evol. , vol.46 , pp. 84-101
    • Axelsen, K.B.1    Palmgren, M.G.2
  • 9
    • 3242701547 scopus 로고    scopus 로고
    • Biology, structure and mechanism of P-type ATPases
    • W. Kuhlbrandt Biology, structure and mechanism of P-type ATPases Nat. Rev. Mol. Cell. Biol. 5 2004 282 295
    • (2004) Nat. Rev. Mol. Cell. Biol. , vol.5 , pp. 282-295
    • Kuhlbrandt, W.1
  • 10
    • 0029940235 scopus 로고    scopus 로고
    • Structural organization, ion transport, and energy transduction of P-type ATPases
    • J.V. Moller, B. Juul, and M. le Maire Structural organization, ion transport, and energy transduction of P-type ATPases Biochim. Biophys. Acta 1286 1996 1 51
    • (1996) Biochim. Biophys. Acta , vol.1286 , pp. 1-51
    • Moller, J.V.1    Juul, B.2    Le Maire, M.3
  • 11
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • C. Toyoshima, and H. Nomura Structural changes in the calcium pump accompanying the dissociation of calcium Nature 418 2002 605 611
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 12
    • 9244232176 scopus 로고    scopus 로고
    • Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues
    • C. Toyoshima, H. Nomura, and T. Tsuda Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues Nature 432 2004 361 368
    • (2004) Nature , vol.432 , pp. 361-368
    • Toyoshima, C.1    Nomura, H.2    Tsuda, T.3
  • 13
    • 3242888769 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump with a bound ATP analogue
    • C. Toyoshima, and T. Mizutani Crystal structure of the calcium pump with a bound ATP analogue Nature 430 2004 529 535
    • (2004) Nature , vol.430 , pp. 529-535
    • Toyoshima, C.1    Mizutani, T.2
  • 14
    • 0018401053 scopus 로고
    • 2+-dependent ATPase of the sarcoplasmic reticulum
    • 2+-dependent ATPase of the sarcoplasmic reticulum Annu. Rev. Biochem. 48 1979 275 292
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 275-292
    • De Meis, L.1    Vianna, A.L.2
  • 15
    • 0015523849 scopus 로고
    • Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase
    • R.L. Post, C. Hegyvary, and S. Kume Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase J. Biol. Chem. 247 1972 6530 6540
    • (1972) J. Biol. Chem. , vol.247 , pp. 6530-6540
    • Post, R.L.1    Hegyvary, C.2    Kume, S.3
  • 17
    • 0033520919 scopus 로고    scopus 로고
    • The rate of activation by calmodulin of isoform 4 of the plasma membrane Ca(2+) pump is slow and is changed by alternative splicing
    • A.J. Caride, N.L. Elwess, A.K. Verma, A.G. Filoteo, A. Enyedi, Z. Bajzer, and J.T. Penniston The rate of activation by calmodulin of isoform 4 of the plasma membrane Ca(2+) pump is slow and is changed by alternative splicing J. Biol. Chem. 274 1999 35227 35232
    • (1999) J. Biol. Chem. , vol.274 , pp. 35227-35232
    • Caride, A.J.1    Elwess, N.L.2    Verma, A.K.3    Filoteo, A.G.4    Enyedi, A.5    Bajzer, Z.6    Penniston, J.T.7
  • 20
    • 0027069575 scopus 로고
    • 2+ pump interacts with the transduction domain of the enzyme
    • 2+ pump interacts with the transduction domain of the enzyme Protein Sci. 1 1992 1613 1621
    • (1992) Protein Sci. , vol.1 , pp. 1613-1621
    • Falchetto, R.1    Vorherr, T.2    Carafoli, E.3
  • 21
    • 0026569304 scopus 로고
    • The plasma membrane calcium pump: A multiregulated transporter
    • K.K. Wang, A. Villalobo, and B.D. Roufogalis The plasma membrane calcium pump: a multiregulated transporter Trends Cell Biol. 2 1992 46 52
    • (1992) Trends Cell Biol. , vol.2 , pp. 46-52
    • Wang, K.K.1    Villalobo, A.2    Roufogalis, B.D.3
  • 24
    • 0032830131 scopus 로고    scopus 로고
    • Effects of reactive oxygen species on brain synaptic plasma membrane Ca(2+)-ATPase
    • A. Zaidi, and M.L. Michaelis Effects of reactive oxygen species on brain synaptic plasma membrane Ca(2+)-ATPase Free Radic. Biol. Med. 27 1999 810 821
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 810-821
    • Zaidi, A.1    Michaelis, M.L.2
  • 26
    • 0034185616 scopus 로고    scopus 로고
    • Protein oxidation and age-dependent alterations in calcium homeostasis
    • T.C. Squier, and D.J. Bigelow Protein oxidation and age-dependent alterations in calcium homeostasis Front. Biosci. 5 2000 D504 D526
    • (2000) Front. Biosci. , vol.5
    • Squier, T.C.1    Bigelow, D.J.2
  • 27
    • 0035066857 scopus 로고    scopus 로고
    • Oxidatively modified calmodulin binds to the plasma membrane Ca-ATPase in a nonproductive and conformationally disordered complex
    • J. Gao, Y. Yao, and T.C. Squier Oxidatively modified calmodulin binds to the plasma membrane Ca-ATPase in a nonproductive and conformationally disordered complex Biophys. J. 80 2001 1791 1801
    • (2001) Biophys. J. , vol.80 , pp. 1791-1801
    • Gao, J.1    Yao, Y.2    Squier, T.C.3
  • 28
    • 15444377616 scopus 로고    scopus 로고
    • A proteomic approach to determination of the significance of protein oxidation in the ageing of mouse hippocampus
    • T. Toda, T. Morimasa, S. Kobayashi, K. Nomura, T. Hatozaki, and M. Hirota A proteomic approach to determination of the significance of protein oxidation in the ageing of mouse hippocampus Appl. Genom. Proteom. 2 2003 43 50
    • (2003) Appl. Genom. Proteom. , vol.2 , pp. 43-50
    • Toda, T.1    Morimasa, T.2    Kobayashi, S.3    Nomura, K.4    Hatozaki, T.5    Hirota, M.6
  • 32
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • S.B. Needleman, and C.D. Wunsch A general method applicable to the search for similarities in the amino acid sequence of two proteins J. Mol. Biol. 48 1970 443 453
    • (1970) J. Mol. Biol. , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 33
    • 0000228203 scopus 로고
    • A model of evolutionary change in proteins: Matrices for detecting distant relationships
    • M. Dayhoff, R.M. Schwartz, and B.C. Orcutt A model of evolutionary change in proteins: matrices for detecting distant relationships Atlas of Protein Sequence and Structure 5 1978 pp. 345-358
    • (1978) Atlas of Protein Sequence and Structure , vol.5
    • Dayhoff, M.1    Schwartz, R.M.2    Orcutt, B.C.3
  • 34
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • C. Toyoshima, M. Nakasako, H. Nomura, and H. Ogawa Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution Nature 405 2000 647 655
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 35
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • T. Schwede, J. Kopp, N. Guex, and M.C. Peitsch SWISS-MODEL: an automated protein homology-modeling server Nucleic Acids Res. 31 2003 3381 3385
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 36
    • 0041571262 scopus 로고    scopus 로고
    • Protein sequence threading by double dynamic programming
    • Elsevier Science New York
    • D.T. Jones Protein sequence threading by double dynamic programming Computational Methods in Molecular Biology 1998 Elsevier Science New York
    • (1998) Computational Methods in Molecular Biology
    • Jones, D.T.1
  • 37
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • L.J. McGuffin, K. Bryson, and D.T. Jones The PSIPRED protein structure prediction server Bioinformatics 16 2000 404 405
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 38
    • 0034697993 scopus 로고    scopus 로고
    • Crystal structure of an archaeal intein-encoded homing endonuclease PI-PfuI
    • K. Ichiyanagi, Y. Ishino, M. Ariyoshi, K. Komori, and K. Morikawa Crystal structure of an archaeal intein-encoded homing endonuclease PI-PfuI J. Mol. Biol. 300 2000 889 901
    • (2000) J. Mol. Biol. , vol.300 , pp. 889-901
    • Ichiyanagi, K.1    Ishino, Y.2    Ariyoshi, M.3    Komori, K.4    Morikawa, K.5
  • 39
    • 0030880594 scopus 로고    scopus 로고
    • Structural analysis of three His32 mutants of DsbA: Support for an electrostatic role of His32 in DsbA stability
    • L.W. Guddat, J.C. Bardwell, R. Glockshuber, M. Huber-Wunderlich, T. Zander, and J.L. Martin Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability Protein Sci. 6 1997 1893 1900
    • (1997) Protein Sci. , vol.6 , pp. 1893-1900
    • Guddat, L.W.1    Bardwell, J.C.2    Glockshuber, R.3    Huber-Wunderlich, M.4    Zander, T.5    Martin, J.L.6
  • 40
    • 0031026207 scopus 로고    scopus 로고
    • The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions
    • J. Lubkowski, G. Bujacz, L. Boque, P.J. Domaille, T.M. Handel, and A. Wlodawer The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions Nat. Struct. Biol. 4 1997 64 69
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 64-69
    • Lubkowski, J.1    Bujacz, G.2    Boque, L.3    Domaille, P.J.4    Handel, T.M.5    Wlodawer, A.6
  • 41
    • 0032763657 scopus 로고    scopus 로고
    • Crystallographic structure of the amino terminal domain of yeast initiation factor 4A, a representative DEAD-box RNA helicase
    • E.R. Johnson, and D.B. McKay Crystallographic structure of the amino terminal domain of yeast initiation factor 4A, a representative DEAD-box RNA helicase RNA 5 1999 1526 1534
    • (1999) RNA , vol.5 , pp. 1526-1534
    • Johnson, E.R.1    McKay, D.B.2
  • 43
    • 0032485628 scopus 로고    scopus 로고
    • Structure of the bis(Mg2+)-ATP-oxalate complex of the rabbit muscle pyruvate kinase at 2.1 Å resolution: ATP binding over a barrel
    • T.M. Larsen, M.M. Benning, I. Rayment, and G.H. Reed Structure of the bis(Mg2+)-ATP-oxalate complex of the rabbit muscle pyruvate kinase at 2.1 Å resolution: ATP binding over a barrel Biochemistry 37 1998 6247 6255
    • (1998) Biochemistry , vol.37 , pp. 6247-6255
    • Larsen, T.M.1    Benning, M.M.2    Rayment, I.3    Reed, G.H.4
  • 44
    • 0027317580 scopus 로고
    • Performance evaluation of amino acid substitution matrices
    • S. Henikoff, and J.G. Henikoff Performance evaluation of amino acid substitution matrices Proteins 17 1993 49 61
    • (1993) Proteins , vol.17 , pp. 49-61
    • Henikoff, S.1    Henikoff, J.G.2
  • 46
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson 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
  • 49
    • 0033587727 scopus 로고    scopus 로고
    • A systematic study of low-resolution recognition in protein-protein complexes
    • I.A. Vakser, O.G. Matar, and C.F. Lam A systematic study of low-resolution recognition in protein-protein complexes Proc. Natl. Acad. Sci. U.S.A. 96 1999 8477 8482
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 8477-8482
    • Vakser, I.A.1    Matar, O.G.2    Lam, C.F.3
  • 53
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?
    • J. Wang, P. Cieplak, and P.A. Kollman How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules? J. Comput. Chem. 21 2000 1049 1074
    • (2000) J. Comput. Chem. , vol.21 , pp. 1049-1074
    • Wang, J.1    Cieplak, P.2    Kollman, P.A.3
  • 54
    • 33748390341 scopus 로고    scopus 로고
    • Parameterized models of aqueous free energies of solvation based on pairwise descreening of solute atomic charges from a dielectric medium
    • G. Hawkins, C.J. Cramer, and D.G. Truhlar Parameterized models of aqueous free energies of solvation based on pairwise descreening of solute atomic charges from a dielectric medium J. Biophys. Chem. 100 1996 19824 19839
    • (1996) J. Biophys. Chem. , vol.100 , pp. 19824-19839
    • Hawkins, G.1    Cramer, C.J.2    Truhlar, D.G.3
  • 56
    • 0000243829 scopus 로고
    • PROCHEK: A program to check the stereochemical quality of protein structures
    • R. Laskowski, M.W. MacArthur, D.S. Moss, and J.M. Thornton PROCHEK: a program to check the stereochemical quality of protein structures J. Appl. Cryst. 26 1993 283 291
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 57
    • 0030598343 scopus 로고    scopus 로고
    • Deviations from standard atomic volumes as a quality measure for protein crystal structures
    • J. Pontius, J. Richelle, and S.J. Wodak Deviations from standard atomic volumes as a quality measure for protein crystal structures J. Mol. Biol. 264 1996 121 136
    • (1996) J. Mol. Biol. , vol.264 , pp. 121-136
    • Pontius, J.1    Richelle, J.2    Wodak, S.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.