메뉴 건너뛰기




Volumn 8, Issue 1, 2013, Pages

A Novel Trans Conformation of Ligand-Free Calmodulin

Author keywords

[No Author keywords available]

Indexed keywords

CALMODULIN;

EID: 84873865235     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0054834     Document Type: Article
Times cited : (17)

References (45)
  • 1
    • 57749181967 scopus 로고    scopus 로고
    • Calmodulin localization and its effects on endocytic and phagocytic membrane trafficking in Paramecium multimicronucleatum
    • Fok AK, Aihara MS, Ishida M, Allen RD, (2008) Calmodulin localization and its effects on endocytic and phagocytic membrane trafficking in Paramecium multimicronucleatum. J Eukaryot Microbiol 55: 481-491.
    • (2008) J Eukaryot Microbiol , vol.55 , pp. 481-491
    • Fok, A.K.1    Aihara, M.S.2    Ishida, M.3    Allen, R.D.4
  • 4
    • 0032708680 scopus 로고    scopus 로고
    • Diversity of conformational states and changes within the EF-hand protein superfamily
    • Yap KL, Ames JB, Swindells MB, Ikura M, (1999) Diversity of conformational states and changes within the EF-hand protein superfamily. Proteins 37: 499-507.
    • (1999) Proteins , vol.37 , pp. 499-507
    • Yap, K.L.1    Ames, J.B.2    Swindells, M.B.3    Ikura, M.4
  • 5
    • 0034257929 scopus 로고    scopus 로고
    • The 1.0 Å crystal structure of Ca(2+)-bound calmodulin: an analysis of disorder and implications for functionally relevant plasticity
    • Wilson MA, Brunger AT, (2000) The 1.0 Å crystal structure of Ca(2+)-bound calmodulin: an analysis of disorder and implications for functionally relevant plasticity. J Mol Biol 301: 1237-1256.
    • (2000) J Mol Biol , vol.301 , pp. 1237-1256
    • Wilson, M.A.1    Brunger, A.T.2
  • 6
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 Å resolution
    • Babu YS, Bugg CE, Cook WJ, (1988) Structure of calmodulin refined at 2.2 Å resolution. J Mol Biol 204: 191-204.
    • (1988) J Mol Biol , vol.204 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 8
    • 0031058901 scopus 로고    scopus 로고
    • Characterization of the basic amphiphilic alpha-helix calmodulin-binding domain of a 61.5 kDa tobacco calmodulin-binding protein
    • Dash S, Niemaczura W, Harrington HM, (1997) Characterization of the basic amphiphilic alpha-helix calmodulin-binding domain of a 61.5 kDa tobacco calmodulin-binding protein. Biochemistry 36: 2025-2029.
    • (1997) Biochemistry , vol.36 , pp. 2025-2029
    • Dash, S.1    Niemaczura, W.2    Harrington, H.M.3
  • 9
    • 0034753415 scopus 로고    scopus 로고
    • Solution structure of Ca(2+)-calmodulin reveals flexible hand-like properties of its domains
    • Chou JJ, Li S, Klee CB, Bax A, (2001) Solution structure of Ca(2+)-calmodulin reveals flexible hand-like properties of its domains. Nat Struct Biol 8: 990-997.
    • (2001) Nat Struct Biol , vol.8 , pp. 990-997
    • Chou, J.J.1    Li, S.2    Klee, C.B.3    Bax, A.4
  • 10
    • 0027759276 scopus 로고
    • Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures
    • Meador WE, Means AR, Quiocho FA, (1993) Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures. Science 262: 1718-1721.
    • (1993) Science , vol.262 , pp. 1718-1721
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 11
    • 80051664755 scopus 로고    scopus 로고
    • Fast methionine-based solution structure determination of calcium-calmodulin complexes
    • Gifford JL, Ishida H, Vogel HJ, (2011) Fast methionine-based solution structure determination of calcium-calmodulin complexes. J Biomol NMR 50: 71-81.
    • (2011) J Biomol NMR , vol.50 , pp. 71-81
    • Gifford, J.L.1    Ishida, H.2    Vogel, H.J.3
  • 12
    • 0037165139 scopus 로고    scopus 로고
    • Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin
    • Drum CL, Yan SZ, Bard J, Shen YQ, Lu D, et al. (2002) Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. Nature 415: 396-402.
    • (2002) Nature , vol.415 , pp. 396-402
    • Drum, C.L.1    Yan, S.Z.2    Bard, J.3    Shen, Y.Q.4    Lu, D.5
  • 13
    • 1842583759 scopus 로고    scopus 로고
    • Structure of anthrax edema factor-calmodulin-adenosine 5'-(alpha,beta-methylene)-triphosphate complex reveals an alternative mode of ATP binding to the catalytic site
    • Shen Y, Guo Q, Zhukovskaya NL, Drum CL, Bohm A, et al. (2004) Structure of anthrax edema factor-calmodulin-adenosine 5'-(alpha,beta-methylene)-triphosphate complex reveals an alternative mode of ATP binding to the catalytic site. Biochem Biophys Res Commun 317: 309-314.
    • (2004) Biochem Biophys Res Commun , vol.317 , pp. 309-314
    • Shen, Y.1    Guo, Q.2    Zhukovskaya, N.L.3    Drum, C.L.4    Bohm, A.5
  • 14
    • 0037450635 scopus 로고    scopus 로고
    • Structural basis for endothelial nitric oxide synthase binding to calmodulin
    • Aoyagi M, Arvai AS, Tainer JA, Getzoff ED, (2003) Structural basis for endothelial nitric oxide synthase binding to calmodulin. Embo Journal 22: 766-775.
    • (2003) Embo Journal , vol.22 , pp. 766-775
    • Aoyagi, M.1    Arvai, A.S.2    Tainer, J.A.3    Getzoff, E.D.4
  • 15
    • 0033592312 scopus 로고    scopus 로고
    • NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump
    • Elshorst B, Hennig M, Forsterling H, Diener A, Maurer M, et al. (1999) NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump. Biochemistry 38: 12320-12332.
    • (1999) Biochemistry , vol.38 , pp. 12320-12332
    • Elshorst, B.1    Hennig, M.2    Forsterling, H.3    Diener, A.4    Maurer, M.5
  • 16
    • 77956150131 scopus 로고    scopus 로고
    • Stoichiometry and topology of the complex of the endogenous ATP synthase inhibitor protein IF(1) with calmodulin
    • Pagnozzi D, Birolo L, Leo G, Contessi S, Lippe G, et al. (2010) Stoichiometry and topology of the complex of the endogenous ATP synthase inhibitor protein IF(1) with calmodulin. Biochemistry 49: 7542-7552.
    • (2010) Biochemistry , vol.49 , pp. 7542-7552
    • Pagnozzi, D.1    Birolo, L.2    Leo, G.3    Contessi, S.4    Lippe, G.5
  • 18
    • 0020512525 scopus 로고
    • Lead and other metals can substitute for Ca2+ in calmodulin
    • Habermann E, Crowell K, Janicki P, (1983) Lead and other metals can substitute for Ca2+ in calmodulin. Archives of toxicology 54: 61-70.
    • (1983) Archives of Toxicology , vol.54 , pp. 61-70
    • Habermann, E.1    Crowell, K.2    Janicki, P.3
  • 19
    • 0021185585 scopus 로고
    • Activation of calmodulin by various metal cations as a function of ionic radius
    • Chao SH, Suzuki Y, Zysk JR, Cheung WY, (1984) Activation of calmodulin by various metal cations as a function of ionic radius. Molecular pharmacology 26: 75-82.
    • (1984) Molecular Pharmacology , vol.26 , pp. 75-82
    • Chao, S.H.1    Suzuki, Y.2    Zysk, J.R.3    Cheung, W.Y.4
  • 21
    • 0033533484 scopus 로고    scopus 로고
    • Battle for the EF-hands: magnesium-calcium interference in calmodulin
    • Malmendal A, Linse S, Evenas J, Forsen S, Drakenberg T, (1999) Battle for the EF-hands: magnesium-calcium interference in calmodulin. Biochemistry 38: 11844-11850.
    • (1999) Biochemistry , vol.38 , pp. 11844-11850
    • Malmendal, A.1    Linse, S.2    Evenas, J.3    Forsen, S.4    Drakenberg, T.5
  • 23
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure
    • Hendrickson WA, Horton JR, LeMaster DM, (1990) Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J 9: 1665-1672.
    • (1990) EMBO J , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    LeMaster, D.M.3
  • 24
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Macromolecular Crystallography, Pt A 276: 307-326.
    • (1997) Macromolecular Crystallography, Pt A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 25
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick GM, (2008) A short history of SHELX. Acta Crystallogr A 64: 112-122.
    • (2008) Acta Crystallogr A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 26
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • Cowtan K, (2006) The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr D Biol Crystallogr 62: 1002-1011.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 27
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 31
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K, (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 32
    • 0028871926 scopus 로고
    • Dali: a network tool for protein structure comparison
    • Holm L, Sander C, (1995) Dali: a network tool for protein structure comparison. Trends Biochem Sci 20: 478-480.
    • (1995) Trends Biochem Sci , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 34
    • 0141594755 scopus 로고    scopus 로고
    • A closed compact structure of native Ca(2+)-calmodulin
    • Fallon JL, Quiocho FA, (2003) A closed compact structure of native Ca(2+)-calmodulin. Structure 11: 1303-1307.
    • (2003) Structure , vol.11 , pp. 1303-1307
    • Fallon, J.L.1    Quiocho, F.A.2
  • 35
    • 28544446450 scopus 로고    scopus 로고
    • Insights into voltage-gated calcium channel regulation from the structure of the CaV1.2 IQ domain-Ca2+/calmodulin complex
    • Van Petegem F, Chatelain FC, Minor DL Jr, (2005) Insights into voltage-gated calcium channel regulation from the structure of the CaV1.2 IQ domain-Ca2+/calmodulin complex. Nature structural & molecular biology 12: 1108-1115.
    • (2005) Nature Structural & Molecular Biology , vol.12 , pp. 1108-1115
    • Van Petegem, F.1    Chatelain, F.C.2    Minor Jr., D.L.3
  • 38
    • 0028960110 scopus 로고
    • Calmodulin stabilizes an amphiphilic alpha-helix within RC3/neurogranin and GAP-43/neuromodulin only when Ca2+ is absent
    • Gerendasy DD, Herron SR, Jennings PA, Sutcliffe JG, (1995) Calmodulin stabilizes an amphiphilic alpha-helix within RC3/neurogranin and GAP-43/neuromodulin only when Ca2+ is absent. The Journal of biological chemistry 270: 6741-6750.
    • (1995) The Journal of Biological Chemistry , vol.270 , pp. 6741-6750
    • Gerendasy, D.D.1    Herron, S.R.2    Jennings, P.A.3    Sutcliffe, J.G.4
  • 39
    • 35548964668 scopus 로고    scopus 로고
    • A 1.3-Å structure of zinc-bound N-terminal domain of calmodulin elucidates potential early ion-binding step
    • Warren JT, Guo Q, Tang WJ, (2007) A 1.3-Å structure of zinc-bound N-terminal domain of calmodulin elucidates potential early ion-binding step. J Mol Biol 374: 517-527.
    • (2007) J Mol Biol , vol.374 , pp. 517-527
    • Warren, J.T.1    Guo, Q.2    Tang, W.J.3
  • 40
    • 11844262754 scopus 로고    scopus 로고
    • Mutation analysis of the histidine residues in the glycylglycine endopeptidase ALE-1
    • Fujiwara T, Aoki S, Komatsuzawa H, Nishida T, Ohara M, et al. (2005) Mutation analysis of the histidine residues in the glycylglycine endopeptidase ALE-1. Journal of bacteriology 187: 480-487.
    • (2005) Journal of Bacteriology , vol.187 , pp. 480-487
    • Fujiwara, T.1    Aoki, S.2    Komatsuzawa, H.3    Nishida, T.4    Ohara, M.5
  • 45
    • 0023644790 scopus 로고
    • Regulation of calmodulin binding to P-57. A neurospecific calmodulin binding protein
    • Alexander KA, Cimler BM, Meier KE, Storm DR, (1987) Regulation of calmodulin binding to P-57. A neurospecific calmodulin binding protein. J Biol Chem 262: 6108-6113.
    • (1987) J Biol Chem , vol.262 , pp. 6108-6113
    • Alexander, K.A.1    Cimler, B.M.2    Meier, K.E.3    Storm, D.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.