메뉴 건너뛰기




Volumn 107, Issue 7, 2014, Pages 1675-1685

Computational studies of the effect of the S23D/S24D troponin i mutation on cardiac troponin structural dynamics

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; MUTANT PROTEIN; PROTEIN SUBUNIT; TROPONIN C; TROPONIN I;

EID: 84908220236     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2014.08.008     Document Type: Article
Times cited : (47)

References (48)
  • 1
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • A.M. Gordon, E. Homsher, and M. Regnier Regulation of contraction in striated muscle Physiol. Rev. 80 2000 853 924
    • (2000) Physiol. Rev. , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 2
    • 34247642743 scopus 로고    scopus 로고
    • Effects of thin and thick filament proteins on calcium binding and exchange with cardiac troponin C
    • J.P. Davis, and C. Norman S.B. Tikunova Effects of thin and thick filament proteins on calcium binding and exchange with cardiac troponin C Biophys. J. 92 2007 3195 3206
    • (2007) Biophys. J. , vol.92 , pp. 3195-3206
    • Davis, J.P.1    Norman, C.2    Tikunova, S.B.3
  • 3
    • 0029031198 scopus 로고
    • The troponin complex and regulation of muscle contraction
    • C.S. Farah, and F.C. Reinach The troponin complex and regulation of muscle contraction FASEB J. 9 1995 755 767
    • (1995) FASEB J. , vol.9 , pp. 755-767
    • Farah, C.S.1    Reinach, F.C.2
  • 4
    • 0029037870 scopus 로고
    • Cardiac troponin i phosphorylation increases the rate of cardiac muscle relaxation
    • R. Zhang, and J. Zhao J.D. Potter Cardiac troponin I phosphorylation increases the rate of cardiac muscle relaxation Circ. Res. 76 1995 1028 1035
    • (1995) Circ. Res. , vol.76 , pp. 1028-1035
    • Zhang, R.1    Zhao, J.2    Potter, J.D.3
  • 5
    • 0035947749 scopus 로고    scopus 로고
    • Phosphorylation of troponin i by protein kinase A accelerates relaxation and crossbridge cycle kinetics in mouse ventricular muscle
    • J.C. Kentish, and D.T. McCloskey R.J. Solaro Phosphorylation of troponin I by protein kinase A accelerates relaxation and crossbridge cycle kinetics in mouse ventricular muscle Circ. Res. 88 2001 1059 1065
    • (2001) Circ. Res. , vol.88 , pp. 1059-1065
    • Kentish, J.C.1    McCloskey, D.T.2    Solaro, R.J.3
  • 6
    • 0034629430 scopus 로고    scopus 로고
    • Cardiac troponin i inhibitory peptide: Location of interaction sites on troponin C
    • M.B. Abbott, and A. Dvoretsky P.R. Rosevear Cardiac troponin I inhibitory peptide: location of interaction sites on troponin C FEBS Lett. 469 2000 168 172
    • (2000) FEBS Lett. , vol.469 , pp. 168-172
    • Abbott, M.B.1    Dvoretsky, A.2    Rosevear, P.R.3
  • 7
    • 40849096222 scopus 로고    scopus 로고
    • The unique functions of cardiac troponin i in the control of cardiac muscle contraction and relaxation
    • R.J. Solaro, P. Rosevear, and T. Kobayashi The unique functions of cardiac troponin I in the control of cardiac muscle contraction and relaxation Biochem. Biophys. Res. Commun. 369 2008 82 87
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 82-87
    • Solaro, R.J.1    Rosevear, P.2    Kobayashi, T.3
  • 9
    • 0030856717 scopus 로고    scopus 로고
    • Calcium-induced structural transition in the regulatory domain of human cardiac troponin C
    • L. Spyracopoulos, and M.X. Li B.D. Sykes Calcium-induced structural transition in the regulatory domain of human cardiac troponin C Biochemistry 36 1997 12138 12146
    • (1997) Biochemistry , vol.36 , pp. 12138-12146
    • Spyracopoulos, L.1    Li, M.X.2    Sykes, B.D.3
  • 10
    • 0033614841 scopus 로고    scopus 로고
    • Binding of cardiac troponin-I147-163 induces a structural opening in human cardiac troponin-C
    • M.X. Li, L. Spyracopoulos, and B.D. Sykes Binding of cardiac troponin-I147-163 induces a structural opening in human cardiac troponin-C Biochemistry 38 1999 8289 8298
    • (1999) Biochemistry , vol.38 , pp. 8289-8298
    • Li, M.X.1    Spyracopoulos, L.2    Sykes, B.D.3
  • 12
    • 84867637621 scopus 로고    scopus 로고
    • Long-timescale molecular dynamics simulations elucidate the dynamics and kinetics of exposure of the hydrophobic patch in troponin C
    • S. Lindert, P.M. Kekenes-Huskey, and J.A. McCammon Long-timescale molecular dynamics simulations elucidate the dynamics and kinetics of exposure of the hydrophobic patch in troponin C Biophys. J. 103 2012 1784 1789
    • (2012) Biophys. J. , vol.103 , pp. 1784-1789
    • Lindert, S.1    Kekenes-Huskey, P.M.2    McCammon, J.A.3
  • 13
    • 84870693969 scopus 로고    scopus 로고
    • Molecular basis of calcium-sensitizing and desensitizing mutations of the human cardiac troponin C regulatory domain: A multi-scale simulation study
    • P.M. Kekenes-Huskey, S. Lindert, and J.A. McCammon Molecular basis of calcium-sensitizing and desensitizing mutations of the human cardiac troponin C regulatory domain: a multi-scale simulation study PLOS Comput. Biol. 8 2012 e1002777
    • (2012) PLOS Comput. Biol. , vol.8 , pp. 1002777
    • Kekenes-Huskey, P.M.1    Lindert, S.2    McCammon, J.A.3
  • 14
    • 84908161688 scopus 로고    scopus 로고
    • Analysis of free energy of opening the troponin C binding pocket for troponin i using microsecond molecular dynamics simulations
    • S. Lindert, P. Kekenes-Huskey, and J.A. McCammon Analysis of free energy of opening the troponin C binding pocket for troponin I using microsecond molecular dynamics simulations Biophys. J. 104 2013 331A 332A
    • (2013) Biophys. J. , vol.104 , pp. 331A-332A
    • Lindert, S.1    Kekenes-Huskey, P.2    McCammon, J.A.3
  • 17
    • 79952586341 scopus 로고    scopus 로고
    • A computational and experimental approach to investigate bepridil binding with cardiac troponin
    • J.F. Varughese, and T. Baxley Y. Li A computational and experimental approach to investigate bepridil binding with cardiac troponin J. Phys. Chem. B 115 2011 2392 2400
    • (2011) J. Phys. Chem. B , vol.115 , pp. 2392-2400
    • Varughese, J.F.1    Baxley, T.2    Li, Y.3
  • 18
    • 79959405666 scopus 로고    scopus 로고
    • Molecular dynamics and docking studies on cardiac troponin C
    • J.F. Varguhese, and Y. Li Molecular dynamics and docking studies on cardiac troponin C J. Biomol. Struct. Dyn. 29 2011 123 135
    • (2011) J. Biomol. Struct. Dyn. , vol.29 , pp. 123-135
    • Varguhese, J.F.1    Li, Y.2
  • 19
    • 77957315736 scopus 로고    scopus 로고
    • Molecular dynamics studies on troponin (TnI-TnT-TnC) complexes: Insight into the regulation of muscle contraction
    • J.F. Varughese, J.M. Chalovich, and Y. Li Molecular dynamics studies on troponin (TnI-TnT-TnC) complexes: insight into the regulation of muscle contraction J. Biomol. Struct. Dyn. 28 2010 159 174
    • (2010) J. Biomol. Struct. Dyn. , vol.28 , pp. 159-174
    • Varughese, J.F.1    Chalovich, J.M.2    Li, Y.3
  • 20
    • 84897800778 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the cardiac troponin complex performed with FRET distances as restraints
    • J.J. Jayasundar, and J. Xing W.-J. Dong Molecular dynamics simulations of the cardiac troponin complex performed with FRET distances as restraints PLoS ONE 9 2014 e87135
    • (2014) PLoS ONE , vol.9 , pp. 87135
    • Jayasundar, J.J.1    Xing, J.2    Dong, W.-J.3
  • 21
    • 34748818674 scopus 로고    scopus 로고
    • Phosphorylation-dependent conformational transition of the cardiac specific N-extension of troponin i in cardiac troponin
    • J.W. Howarth, and J. Meller P.R. Rosevear Phosphorylation-dependent conformational transition of the cardiac specific N-extension of troponin I in cardiac troponin J. Mol. Biol. 373 2007 706 722
    • (2007) J. Mol. Biol. , vol.373 , pp. 706-722
    • Howarth, J.W.1    Meller, J.2    Rosevear, P.R.3
  • 22
    • 0032773882 scopus 로고    scopus 로고
    • NMR analysis of cardiac troponin C-troponin i complexes: Effects of phosphorylation
    • N. Finley, and M.B. Abbott P.R. Rosevear NMR analysis of cardiac troponin C-troponin I complexes: effects of phosphorylation FEBS Lett. 453 1999 107 112
    • (1999) FEBS Lett. , vol.453 , pp. 107-112
    • Finley, N.1    Abbott, M.B.2    Rosevear, P.R.3
  • 23
    • 12844260739 scopus 로고    scopus 로고
    • In vivo and in vitro analysis of cardiac troponin i phosphorylation
    • S. Sakthivel, and N.L. Finley J. Robbins In vivo and in vitro analysis of cardiac troponin I phosphorylation J. Biol. Chem. 280 2005 703 714
    • (2005) J. Biol. Chem. , vol.280 , pp. 703-714
    • Sakthivel, S.1    Finley, N.L.2    Robbins, J.3
  • 24
    • 0029561016 scopus 로고
    • Reconstitution of skinned cardiac fibres with human recombinant cardiac troponin-I mutants and troponin-C
    • C. Dohet, and E. al-Hillawi J.C. Rüegg Reconstitution of skinned cardiac fibres with human recombinant cardiac troponin-I mutants and troponin-C FEBS Lett. 377 1995 131 134
    • (1995) FEBS Lett. , vol.377 , pp. 131-134
    • Dohet, C.1    Al-Hillawi, E.2    Rüegg, J.C.3
  • 25
    • 1542343926 scopus 로고    scopus 로고
    • Frequency- and afterload-dependent cardiac modulation in vivo by troponin i with constitutively active protein kinase A phosphorylation sites
    • E. Takimoto, and D.G. Soergel A.M. Murphy Frequency- and afterload-dependent cardiac modulation in vivo by troponin I with constitutively active protein kinase A phosphorylation sites Circ. Res. 94 2004 496 504
    • (2004) Circ. Res. , vol.94 , pp. 496-504
    • Takimoto, E.1    Soergel, D.G.2    Murphy, A.M.3
  • 26
    • 34249676905 scopus 로고    scopus 로고
    • The troponin C G159D mutation blunts myofilament desensitization induced by troponin i Ser23/24 phosphorylation
    • B.J. Biesiadecki, and T. Kobayashi P.P. de Tombe The troponin C G159D mutation blunts myofilament desensitization induced by troponin I Ser23/24 phosphorylation Circ. Res. 100 2007 1486 1493
    • (2007) Circ. Res. , vol.100 , pp. 1486-1493
    • Biesiadecki, B.J.1    Kobayashi, T.2    De Tombe, P.P.3
  • 27
    • 84884284974 scopus 로고    scopus 로고
    • Length dependence of striated muscle force generation is controlled by phosphorylation of cTnI at serines 23/24
    • L.M. Hanft, B.J. Biesiadecki, and K.S. McDonald Length dependence of striated muscle force generation is controlled by phosphorylation of cTnI at serines 23/24 J. Physiol. 591 2013 4535 4547
    • (2013) J. Physiol. , vol.591 , pp. 4535-4547
    • Hanft, L.M.1    Biesiadecki, B.J.2    McDonald, K.S.3
  • 28
    • 84872425232 scopus 로고    scopus 로고
    • Impact of site-specific phosphorylation of protein kinase A sites Ser23 and Ser24 of cardiac troponin i in human cardiomyocytes
    • P.J.M. Wijnker, and D.B. Foster J. van der Velden Impact of site-specific phosphorylation of protein kinase A sites Ser23 and Ser24 of cardiac troponin I in human cardiomyocytes Am. J. Physiol. Heart Circ. Physiol. 304 2013 H260 H268
    • (2013) Am. J. Physiol. Heart Circ. Physiol. , vol.304 , pp. 260-H268
    • Wijnker, P.J.M.1    Foster, D.B.2    Van Der Velden, J.3
  • 29
    • 84872386336 scopus 로고    scopus 로고
    • N-terminal phosphorylation of cardiac troponin-I reduces length-dependent calcium sensitivity of contraction in cardiac muscle
    • V.S. Rao, and F.S. Korte D.A. Martyn N-terminal phosphorylation of cardiac troponin-I reduces length-dependent calcium sensitivity of contraction in cardiac muscle J. Physiol. 591 2013 475 490
    • (2013) J. Physiol. , vol.591 , pp. 475-490
    • Rao, V.S.1    Korte, F.S.2    Martyn, D.A.3
  • 30
    • 0037076791 scopus 로고    scopus 로고
    • Protein kinase A phosphorylates titin's cardiac-specific N2B domain and reduces passive tension in rat cardiac myocytes
    • R. Yamasaki, and Y. Wu H. Granzier Protein kinase A phosphorylates titin's cardiac-specific N2B domain and reduces passive tension in rat cardiac myocytes Circ. Res. 90 2002 1181 1188
    • (2002) Circ. Res. , vol.90 , pp. 1181-1188
    • Yamasaki, R.1    Wu, Y.2    Granzier, H.3
  • 31
    • 53549129239 scopus 로고    scopus 로고
    • Protein kinase A-mediated phosphorylation of cMyBP-C increases proximity of myosin heads to actin in resting myocardium
    • B.A. Colson, and T. Bekyarova R.L. Moss Protein kinase A-mediated phosphorylation of cMyBP-C increases proximity of myosin heads to actin in resting myocardium Circ. Res. 103 2008 244 251
    • (2008) Circ. Res. , vol.103 , pp. 244-251
    • Colson, B.A.1    Bekyarova, T.2    Moss, R.L.3
  • 32
    • 2442449534 scopus 로고    scopus 로고
    • Modeling structurally variable regions in homologous proteins with rosetta
    • C.A. Rohl, and C.E.M. Strauss D. Baker Modeling structurally variable regions in homologous proteins with rosetta Proteins 55 2004 656 677
    • (2004) Proteins , vol.55 , pp. 656-677
    • Rohl, C.A.1    Strauss, C.E.M.2    Baker, D.3
  • 33
    • 33644949935 scopus 로고    scopus 로고
    • Recapitulation and design of protein binding peptide structures and sequences
    • V.D. Sood, and D. Baker Recapitulation and design of protein binding peptide structures and sequences J. Mol. Biol. 357 2006 917 927
    • (2006) J. Mol. Biol. , vol.357 , pp. 917-927
    • Sood, V.D.1    Baker, D.2
  • 34
    • 0030004861 scopus 로고    scopus 로고
    • Thin filament-mediated regulation of cardiac contraction
    • L.S. Tobacman Thin filament-mediated regulation of cardiac contraction Annu. Rev. Physiol. 58 1996 447 481
    • (1996) Annu. Rev. Physiol. , vol.58 , pp. 447-481
    • Tobacman, L.S.1
  • 37
    • 0242593434 scopus 로고    scopus 로고
    • Development and current status of the CHARMM force field for nucleic acids
    • A.D. MacKerell Jr., N. Banavali, and N. Foloppe Development and current status of the CHARMM force field for nucleic acids Biopolymers 56 2000-2001 257 265
    • (2000) Biopolymers , vol.56 , pp. 257-265
    • Mackerell, A.D.1    Banavali, N.2    Foloppe, N.3
  • 39
    • 33846823909 scopus 로고
    • Particle mesh Ewald - An N•log(N) method for Ewald sums in large systems
    • T. Darden, D. York, and L. Pedersen Particle mesh Ewald - an N•log(N) method for Ewald sums in large systems J. Chem. Phys. 98 1993 10089 10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 40
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • J.-P. Ryckaert, G. Ciccotti, and H.J.C. Berendsen Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes J. Comput. Phys. 23 1977 327 341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 41
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • B. Lee, and F.M. Richards The interpretation of protein structures: estimation of static accessibility J. Mol. Biol. 55 1971 379 400
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 42
    • 42049094204 scopus 로고    scopus 로고
    • Role of the acidic N′ region of cardiac troponin i in regulating myocardial function
    • S. Sadayappan, and N. Finley J. Robbins Role of the acidic N′ region of cardiac troponin I in regulating myocardial function FASEB J. 22 2008 1246 1257
    • (2008) FASEB J. , vol.22 , pp. 1246-1257
    • Sadayappan, S.1    Finley, N.2    Robbins, J.3
  • 43
    • 0030904641 scopus 로고    scopus 로고
    • Phosphorylation-induced distance change in a cardiac muscle troponin i mutant
    • W.J. Dong, and M. Chandra H.C. Cheung Phosphorylation-induced distance change in a cardiac muscle troponin I mutant Biochemistry 36 1997 6754 6761
    • (1997) Biochemistry , vol.36 , pp. 6754-6761
    • Dong, W.J.1    Chandra, M.2    Cheung, H.C.3
  • 44
    • 0038001419 scopus 로고    scopus 로고
    • Small-angle neutron scattering with contrast variation reveals spatial relationships between the three subunits in the ternary cardiac troponin complex and the effects of troponin i phosphorylation
    • W.T. Heller, and N.L. Finley J. Trewhella Small-angle neutron scattering with contrast variation reveals spatial relationships between the three subunits in the ternary cardiac troponin complex and the effects of troponin I phosphorylation Biochemistry 42 2003 7790 7800
    • (2003) Biochemistry , vol.42 , pp. 7790-7800
    • Heller, W.T.1    Finley, N.L.2    Trewhella, J.3
  • 45
    • 0032578421 scopus 로고    scopus 로고
    • Stepwise subunit interaction changes by mono- and bisphosphorylation of cardiac troponin i
    • S.U. Reiffert, and K. Jaquet F.W. Herberg Stepwise subunit interaction changes by mono- and bisphosphorylation of cardiac troponin I Biochemistry 37 1998 13516 13525
    • (1998) Biochemistry , vol.37 , pp. 13516-13525
    • Reiffert, S.U.1    Jaquet, K.2    Herberg, F.W.3
  • 46
    • 33750438825 scopus 로고    scopus 로고
    • Impaired diastolic function after exchange of endogenous troponin i with C-terminal truncated troponin i in human cardiac muscle
    • N.A. Narolska, and N. Piroddi G.J.M. Stienen Impaired diastolic function after exchange of endogenous troponin I with C-terminal truncated troponin I in human cardiac muscle Circ. Res. 99 2006 1012 1020
    • (2006) Circ. Res. , vol.99 , pp. 1012-1020
    • Narolska, N.A.1    Piroddi, N.2    Stienen, G.J.M.3
  • 47
    • 78650848080 scopus 로고    scopus 로고
    • Calcium binding kinetics of troponin C strongly modulate cooperative activation and tension kinetics in cardiac muscle
    • K.L. Kreutziger, and N. Piroddi M. Regnier Calcium binding kinetics of troponin C strongly modulate cooperative activation and tension kinetics in cardiac muscle J. Mol. Cell. Cardiol. 50 2011 165 174
    • (2011) J. Mol. Cell. Cardiol. , vol.50 , pp. 165-174
    • Kreutziger, K.L.1    Piroddi, N.2    Regnier, M.3
  • 48
    • 0037687332 scopus 로고    scopus 로고
    • Phosphorylation or glutamic acid substitution at protein kinase C sites on cardiac troponin i differentially depress myofilament tension and shortening velocity
    • E.M. Burkart, and M.P. Sumandea R.J. Solaro Phosphorylation or glutamic acid substitution at protein kinase C sites on cardiac troponin I differentially depress myofilament tension and shortening velocity J. Biol. Chem. 278 2003 11265 11272
    • (2003) J. Biol. Chem. , vol.278 , pp. 11265-11272
    • Burkart, E.M.1    Sumandea, M.P.2    Solaro, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.