메뉴 건너뛰기




Volumn 80, Issue 8, 2012, Pages 1998-2008

Inhibition of interdomain motion in g-actin by the natural product latrunculin: A molecular dynamics study

Author keywords

Actin; Conformational transition; Domain rotation; Latrunculin; Motional correlation

Indexed keywords

ADENOSINE TRIPHOSPHATE; G ACTIN; LATRUNCULIN A;

EID: 84863779713     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24088     Document Type: Article
Times cited : (13)

References (48)
  • 1
    • 0032437666 scopus 로고    scopus 로고
    • Signaling to the actin cytoskeleton
    • Schmidt A, Hall MN. Signaling to the actin cytoskeleton. Annu Rev Cell Dev Biol 1998; 14: 305-338.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 305-338
    • Schmidt, A.1    Hall, M.N.2
  • 2
    • 0032006059 scopus 로고    scopus 로고
    • Microtubules and actin filaments: dynamic targets for cancer chemotherapy
    • Jordan MA, Wilson L. Microtubules and actin filaments: dynamic targets for cancer chemotherapy. Curr Opin Cell Biol 1998; 10: 123-130.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 123-130
    • Jordan, M.A.1    Wilson, L.2
  • 3
    • 0028899770 scopus 로고
    • Medical aspects of the actin cytoskeleton
    • Janmey PA, Chaponnier C. Medical aspects of the actin cytoskeleton. Curr Opin Cell Biol 1995; 7: 111-117.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 111-117
    • Janmey, P.A.1    Chaponnier, C.2
  • 4
    • 0642286487 scopus 로고    scopus 로고
    • The actin cytoskeleton as a therapeutic target: state of the art and future directions
    • Giganti A, Friederich E. The actin cytoskeleton as a therapeutic target: state of the art and future directions. Prog Cell Cycle Res 2003; 5: 511-525.
    • (2003) Prog Cell Cycle Res , vol.5 , pp. 511-525
    • Giganti, A.1    Friederich, E.2
  • 5
    • 2942564379 scopus 로고    scopus 로고
    • The actin cytoskeleton in normal and pathological cell motility
    • Lambrechts A, Van Troys M, Ampe C. The actin cytoskeleton in normal and pathological cell motility. Int J Biochem Cell Biol 2004; 36: 1890-1909.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 1890-1909
    • Lambrechts, A.1    Van Troys, M.2    Ampe, C.3
  • 8
    • 0000986243 scopus 로고
    • Isolation of a new toxin from the sponge Latrunculia magnifica in the Gulf of Aquaba (Red Sea)
    • Nèeman I, Fishelson L, Kashman Y. Isolation of a new toxin from the sponge Latrunculia magnifica in the Gulf of Aquaba (Red Sea). Mar Biol 1975; 30: 293-296.
    • (1975) Mar Biol , vol.30 , pp. 293-296
    • Nèeman, I.1    Fishelson, L.2    Kashman, Y.3
  • 9
    • 0033775855 scopus 로고    scopus 로고
    • Latrunculin alters the actin-monomer subunit interface to prevent polymerization
    • Morton WM, Ayscough KR, McLaughlin PJ. Latrunculin alters the actin-monomer subunit interface to prevent polymerization. Nat Cell Biol 2000; 2: 376-378.
    • (2000) Nat Cell Biol , vol.2 , pp. 376-378
    • Morton, W.M.1    Ayscough, K.R.2    McLaughlin, P.J.3
  • 10
    • 0032829103 scopus 로고    scopus 로고
    • New anti-actin drugs in the study of the organization and function of the actin cytoskeleton
    • Spector I, Braet F, Shochet NR, Bubb MR. New anti-actin drugs in the study of the organization and function of the actin cytoskeleton. Microsc Res Tech 1999; 47: 18-37.
    • (1999) Microsc Res Tech , vol.47 , pp. 18-37
    • Spector, I.1    Braet, F.2    Shochet, N.R.3    Bubb, M.R.4
  • 11
    • 0027267312 scopus 로고
    • Evaluation of marine sponge metabolites for cytotoxicity and signal transduction activity
    • Longley RE, McConnell OJ, Essich E, Harmody D. Evaluation of marine sponge metabolites for cytotoxicity and signal transduction activity. J Nat Prod 1993; 56: 915-920.
    • (1993) J Nat Prod , vol.56 , pp. 915-920
    • Longley, R.E.1    McConnell, O.J.2    Essich, E.3    Harmody, D.4
  • 14
    • 75749095171 scopus 로고    scopus 로고
    • Semisynthetic latrunculin derivatives as inhibitors of metastatic breast cancer: biological evaluations, preliminary structure-activity relationship and molecular modeling studies
    • Khanfar MA, Youssef DTA, El Sayed KA. Semisynthetic latrunculin derivatives as inhibitors of metastatic breast cancer: biological evaluations, preliminary structure-activity relationship and molecular modeling studies. ChemMedChem 2010; 5: 274-285.
    • (2010) ChemMedChem , vol.5 , pp. 274-285
    • Khanfar, M.A.1    Youssef, D.T.A.2    El Sayed, K.A.3
  • 15
    • 0033845469 scopus 로고    scopus 로고
    • Effect of latrunculin B on outflow facility in monkeys
    • Peterson JA, Tian B, Geiger B, Kaufman PL. Effect of latrunculin B on outflow facility in monkeys. Exp Eye Res 2000; 70: 307-313.
    • (2000) Exp Eye Res , vol.70 , pp. 307-313
    • Peterson, J.A.1    Tian, B.2    Geiger, B.3    Kaufman, P.L.4
  • 16
    • 20444420894 scopus 로고    scopus 로고
    • Diverted total synthesis: preparation of a focused library of latrunculin analogues and evaluation of their actin-binding properties
    • Fürstner A, Kirk D, Fenster MD, Aïssa C, De Souza D, Müller O. Diverted total synthesis: preparation of a focused library of latrunculin analogues and evaluation of their actin-binding properties. Proc Natl Acad Sci USA 2005; 102: 8103-8108.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8103-8108
    • Fürstner, A.1    Kirk, D.2    Fenster, M.D.3    Aïssa, C.4    De Souza, D.5    Müller, O.6
  • 17
    • 33845951511 scopus 로고    scopus 로고
    • Latrunculin analogues with improved biological profiles by "Diverted otal Synthesis": preparation, evaluation, and computational analysis
    • Fürstner A, Kirk D, Fenster MD, Aïssa C, De Souza D, Nevado C, Tuttle T, Thiel W, Müller O. Latrunculin analogues with improved biological profiles by "Diverted otal Synthesis": preparation, evaluation, and computational analysis. Chem Eur J 2007; 13: 135-149.
    • (2007) Chem Eur J , vol.13 , pp. 135-149
    • Fürstner, A.1    Kirk, D.2    Fenster, M.D.3    Aïssa, C.4    De Souza, D.5    Nevado, C.6    Tuttle, T.7    Thiel, W.8    Müller, O.9
  • 18
    • 56749165108 scopus 로고    scopus 로고
    • Interrogating the bioactive pharmacophore of the latrunculin chemotype by investigating the metabolites of two taxonomically unrelated sponges
    • Amagata T, Johnson TA, Cichewicz RH, Tenney K, Mooberry SL, Media J, Edelstein M, Valeriote FA, Crews P. Interrogating the bioactive pharmacophore of the latrunculin chemotype by investigating the metabolites of two taxonomically unrelated sponges. J Med Chem 2008; 51: 7234-7242.
    • (2008) J Med Chem , vol.51 , pp. 7234-7242
    • Amagata, T.1    Johnson, T.A.2    Cichewicz, R.H.3    Tenney, K.4    Mooberry, S.L.5    Media, J.6    Edelstein, M.7    Valeriote, F.A.8    Crews, P.9
  • 19
    • 58749091822 scopus 로고    scopus 로고
    • The nature of the globular- to fibrous-actin transition
    • Oda T, Iwasa M, Aihara T, Maéda Y, Narita A. The nature of the globular- to fibrous-actin transition. Nature 2009; 457: 441-445.
    • (2009) Nature , vol.457 , pp. 441-445
    • Oda, T.1    Iwasa, M.2    Aihara, T.3    Maéda, Y.4    Narita, A.5
  • 20
    • 77957996302 scopus 로고    scopus 로고
    • Direct visualization of secondary structures of F-actin by electron cryomicroscopy
    • Fujii T, Iwane AH, Yanagida T, Namba K. Direct visualization of secondary structures of F-actin by electron cryomicroscopy. Nature 2010; 467: 724-728.
    • (2010) Nature , vol.467 , pp. 724-728
    • Fujii, T.1    Iwane, A.H.2    Yanagida, T.3    Namba, K.4
  • 24
    • 34548226450 scopus 로고    scopus 로고
    • Nucleotide effects on the structure and dynamics of actin
    • Zheng X, Diraviyam K, Sept D. Nucleotide effects on the structure and dynamics of actin. Biophys J 2007; 93: 1277-1283.
    • (2007) Biophys J , vol.93 , pp. 1277-1283
    • Zheng, X.1    Diraviyam, K.2    Sept, D.3
  • 25
    • 38049081531 scopus 로고    scopus 로고
    • Nucleotide-mediated conformational changes of monomeric actin and Arp3 studied by molecular dynamics simulations
    • Dalhaimer P, Pollard TD, Nolen BJ. Nucleotide-mediated conformational changes of monomeric actin and Arp3 studied by molecular dynamics simulations. J Mol Biol 2008; 376: 166-183.
    • (2008) J Mol Biol , vol.376 , pp. 166-183
    • Dalhaimer, P.1    Pollard, T.D.2    Nolen, B.J.3
  • 26
    • 77449087878 scopus 로고    scopus 로고
    • Nucleotide-dependence of G-actin conformation from multiple molecular dynamics simulations and observation of a putatively polymerization-competent superclosed state
    • Splettstoesser T, Noé F, Oda T, Smith JC. Nucleotide-dependence of G-actin conformation from multiple molecular dynamics simulations and observation of a putatively polymerization-competent superclosed state. Proteins: Struct Funct Bioinform 2009; 76: 353-364.
    • (2009) Proteins: Struct Funct Bioinform , vol.76 , pp. 353-364
    • Splettstoesser, T.1    Noé, F.2    Oda, T.3    Smith, J.C.4
  • 27
    • 33646189384 scopus 로고    scopus 로고
    • The open nucleotide pocket of the profilin/actin X-ray structure is unstable and closes in the absence of profilin
    • Minehardt TJ, Kollman PA, Cooke R, Pate E. The open nucleotide pocket of the profilin/actin X-ray structure is unstable and closes in the absence of profilin. Biophys J 2006; 90: 2445-2449.
    • (2006) Biophys J , vol.90 , pp. 2445-2449
    • Minehardt, T.J.1    Kollman, P.A.2    Cooke, R.3    Pate, E.4
  • 29
    • 80053300417 scopus 로고    scopus 로고
    • Water molecules in the nucleotide binding cleft of actin: effects on subunit conformation and implications for ATP hydrolysis
    • Saunders MG, Voth GA. Water molecules in the nucleotide binding cleft of actin: effects on subunit conformation and implications for ATP hydrolysis. J Mol Biol 2011; 413: 279-291.
    • (2011) J Mol Biol , vol.413 , pp. 279-291
    • Saunders, M.G.1    Voth, G.A.2
  • 31
    • 0027251071 scopus 로고
    • Structure of gelsolin segment 1-actin complex and the mechanism of filament severing
    • McLaughlin PJ, Gooch JT, Mannherz HG, Weeds AG. Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature 1993; 364: 685-692.
    • (1993) Nature , vol.364 , pp. 685-692
    • McLaughlin, P.J.1    Gooch, J.T.2    Mannherz, H.G.3    Weeds, A.G.4
  • 32
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold K, Bordoli L, Kopp J, Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 2006; 22: 195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 40
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equation of motion of a system with constraints: molecular dynamics of n-alkanes
    • Ryckaert JP, Ciccotti G, Berendsen HJC. Numerical integration of the cartesian equation of motion of a system with constraints: molecular dynamics of n-alkanes. J Comput Phys 1977; 23: 327-341.
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 41
    • 77954649029 scopus 로고    scopus 로고
    • Multiple conformations of F-actin
    • Oda T, Maéda Y. Multiple conformations of F-actin. Structure 2010; 18: 761-767.
    • (2010) Structure , vol.18 , pp. 761-767
    • Oda, T.1    Maéda, Y.2
  • 42
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme
    • Hayward S, Berendsen HJC. Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme. Proteins: Struct Funct Genet 1998; 30: 144-154.
    • (1998) Proteins: Struct Funct Genet , vol.30 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.C.2
  • 44
    • 79952498871 scopus 로고    scopus 로고
    • Wordom: a user-friendly program for the analysis of molecular structures, trajectories, and free energy surfaces
    • Seeber M, Felline A, Raimondi F, Muff S, Friedman R, Rao F, Caflisch A, Fanelli F. Wordom: a user-friendly program for the analysis of molecular structures, trajectories, and free energy surfaces. J Comput Chem 2011; 32: 1183-1194.
    • (2011) J Comput Chem , vol.32 , pp. 1183-1194
    • Seeber, M.1    Felline, A.2    Raimondi, F.3    Muff, S.4    Friedman, R.5    Rao, F.6    Caflisch, A.7    Fanelli, F.8
  • 47
    • 2442709103 scopus 로고    scopus 로고
    • Non-muscle actin filament elongation from complexes of profilin with nucleotide-free actin and divalent cation-free ATP-actin
    • Kinosian HJ, Selden LA, Gershman LC, Estes JE. Non-muscle actin filament elongation from complexes of profilin with nucleotide-free actin and divalent cation-free ATP-actin. Biochemistry 2004; 43: 6253-6260.
    • (2004) Biochemistry , vol.43 , pp. 6253-6260
    • Kinosian, H.J.1    Selden, L.A.2    Gershman, L.C.3    Estes, J.E.4
  • 48
    • 42149174453 scopus 로고    scopus 로고
    • Fragment-based de novo ligand design by multiobjective evolutionary optimization
    • Dey F, Caflisch A. Fragment-based de novo ligand design by multiobjective evolutionary optimization. J Chem Inf Model 2008; 48: 679-690.
    • (2008) J Chem Inf Model , vol.48 , pp. 679-690
    • Dey, F.1    Caflisch, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.