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Volumn 20, Issue 7, 2012, Pages 1167-1176

Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALMODULIN; FIBROBLAST GROWTH FACTOR; VOLTAGE GATED SODIUM CHANNEL;

EID: 84863534231     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.05.001     Document Type: Article
Times cited : (131)

References (55)
  • 6
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • DOI 10.1006/jmbi.1998.1843
    • A.A. Bogan, and K.S. Thorn Anatomy of hot spots in protein interfaces J. Mol. Biol. 280 1998 1 9 (Pubitemid 28312802)
    • (1998) Journal of Molecular Biology , vol.280 , Issue.1 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 8
    • 79151482756 scopus 로고    scopus 로고
    • Solution NMR structure of Apo-calmodulin in complex with the IQ motif of human cardiac sodium channel NaV1.5
    • B. Chagot, and W.J. Chazin Solution NMR structure of Apo-calmodulin in complex with the IQ motif of human cardiac sodium channel NaV1.5 J. Mol. Biol. 406 2011 106 119
    • (2011) J. Mol. Biol. , vol.406 , pp. 106-119
    • Chagot, B.1    Chazin, W.J.2
  • 9
    • 65249136569 scopus 로고    scopus 로고
    • Solution NMR structure of the C-terminal EF-hand domain of human cardiac sodium channel NaV1.5
    • B. Chagot, F. Potet, J.R. Balser, and W.J. Chazin Solution NMR structure of the C-terminal EF-hand domain of human cardiac sodium channel NaV1.5 J. Biol. Chem. 284 2009 6436 6445
    • (2009) J. Biol. Chem. , vol.284 , pp. 6436-6445
    • Chagot, B.1    Potet, F.2    Balser, J.R.3    Chazin, W.J.4
  • 10
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • T. Clackson, and J.A. Wells A hot spot of binding energy in a hormone-receptor interface Science 267 1995 383 386
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 12
    • 79955816232 scopus 로고    scopus 로고
    • Structural and energetic determinants of apo calmodulin binding to the IQ motif of the Na(V)1.2 voltage-dependent sodium channel
    • M.D. Feldkamp, L. Yu, and M.A. Shea Structural and energetic determinants of apo calmodulin binding to the IQ motif of the Na(V)1.2 voltage-dependent sodium channel Structure 19 2011 733 747
    • (2011) Structure , vol.19 , pp. 733-747
    • Feldkamp, M.D.1    Yu, L.2    Shea, M.A.3
  • 14
    • 67650533766 scopus 로고    scopus 로고
    • Crystal structure of a fibroblast growth factor homologous factor (FHF) defines a conserved surface on FHFs for binding and modulation of voltage-gated sodium channels
    • R. Goetz, K. Dover, F. Laezza, N. Shtraizent, X. Huang, D. Tchetchik, A.V. Eliseenkova, C.F. Xu, T.A. Neubert, and D.M. Ornitz Crystal structure of a fibroblast growth factor homologous factor (FHF) defines a conserved surface on FHFs for binding and modulation of voltage-gated sodium channels J. Biol. Chem. 284 2009 17883 17896
    • (2009) J. Biol. Chem. , vol.284 , pp. 17883-17896
    • Goetz, R.1    Dover, K.2    Laezza, F.3    Shtraizent, N.4    Huang, X.5    Tchetchik, D.6    Eliseenkova, A.V.7    Xu, C.F.8    Neubert, T.A.9    Ornitz, D.M.10
  • 17
    • 0141856484 scopus 로고    scopus 로고
    • vl.6 and differentially modulates their functional properties
    • R.I. Herzog, C. Liu, S.G. Waxman, and T.R. Cummins Calmodulin binds to the C terminus of sodium channels Nav1.4 and Nav1.6 and differentially modulates their functional properties J. Neurosci. 23 2003 8261 8270 (Pubitemid 37129643)
    • (2003) Journal of Neuroscience , vol.23 , Issue.23 , pp. 8261-8270
    • Herzog, R.I.1    Liu, C.2    Waxman, S.G.3    Cummins, T.R.4
  • 18
    • 0028987938 scopus 로고
    • Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor
    • P. Hidalgo, and R. MacKinnon Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor Science 268 1995 307 310
    • (1995) Science , vol.268 , pp. 307-310
    • Hidalgo, P.1    MacKinnon, R.2
  • 23
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • DOI 10.1006/jmbi.1993.1648
    • M.C. Lawrence, and P.M. Colman Shape complementarity at protein/protein interfaces J. Mol. Biol. 234 1993 946 950 (Pubitemid 24027225)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.4 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 25
    • 0035378502 scopus 로고    scopus 로고
    • Fibroblast growth factor homologous factor 1B binds to the C terminus of the tetrodotoxin-resistant sodium channel rNav1.9a (NaN)
    • C.J. Liu, S.D. Dib-Hajj, and S.G. Waxman Fibroblast growth factor homologous factor 1B binds to the C terminus of the tetrodotoxin-resistant sodium channel rNav1.9a (NaN) J. Biol. Chem. 276 2001 18925 18933
    • (2001) J. Biol. Chem. , vol.276 , pp. 18925-18933
    • Liu, C.J.1    Dib-Hajj, S.D.2    Waxman, S.G.3
  • 27
    • 77249103939 scopus 로고    scopus 로고
    • Enzyme-inhibitor-like tuning of Ca(2+) channel connectivity with calmodulin
    • X. Liu, P.S. Yang, W. Yang, and D.T. Yue Enzyme-inhibitor-like tuning of Ca(2+) channel connectivity with calmodulin Nature 463 2010 968 972
    • (2010) Nature , vol.463 , pp. 968-972
    • Liu, X.1    Yang, P.S.2    Yang, W.3    Yue, D.T.4
  • 28
    • 23244441222 scopus 로고    scopus 로고
    • Voltage sensor of Kv1.2: Structural basis of electromechanical coupling
    • DOI 10.1126/science.1116270
    • S.B. Long, E.B. Campbell, and R. Mackinnon Voltage sensor of Kv1.2: structural basis of electromechanical coupling Science 309 2005 903 908 (Pubitemid 41099920)
    • (2005) Science , vol.309 , Issue.5736 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 29
    • 58249130592 scopus 로고    scopus 로고
    • A catalog of SCN1A variants
    • C. Lossin A catalog of SCN1A variants Brain Dev. 31 2009 114 130
    • (2009) Brain Dev. , vol.31 , pp. 114-130
    • Lossin, C.1
  • 32
    • 77954514571 scopus 로고    scopus 로고
    • Sodium channel gene family: Epilepsy mutations, gene interactions and modifier effects
    • M.H. Meisler, J.E. O'Brien, and L.M. Sharkey Sodium channel gene family: epilepsy mutations, gene interactions and modifier effects J. Physiol. 588 2010 1841 1848
    • (2010) J. Physiol. , vol.588 , pp. 1841-1848
    • Meisler, M.H.1    O'Brien, J.E.2    Sharkey, L.M.3
  • 35
    • 33749665782 scopus 로고    scopus 로고
    • Nonfunctional SCN1A is common in severe myoclonic epilepsy of infancy
    • DOI 10.1111/j.1528-1167.2006.00643.x
    • I. Ohmori, K.M. Kahlig, T.H. Rhodes, D.W. Wang, and A.L. George Jr. Nonfunctional SCN1A is common in severe myoclonic epilepsy of infancy Epilepsia 47 2006 1636 1642 (Pubitemid 44556397)
    • (2006) Epilepsia , vol.47 , Issue.10 , pp. 1636-1642
    • Ohmori, I.1    Kahlig, K.M.2    Rhodes, T.H.3    Wang, D.W.4    George Jr., A.L.5
  • 37
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode C.W. Carter Jr. R.M. Sweet, Methods in Enzymology 1997 Academic Press New York 307 326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • J. Payandeh, T. Scheuer, N. Zheng, and W.A. Catterall The crystal structure of a voltage-gated sodium channel Nature 475 2011 353 358
    • (2011) Nature , vol.475 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 39
    • 79960675601 scopus 로고    scopus 로고
    • Facilitation and Ca2+-dependent inactivation are modified by mutation of the Ca(v)1.2 channel IQ motif
    • M. Poomvanicha, J.W. Wegener, A. Blaich, S. Fischer, K. Domes, S. Moosmang, and F. Hofmann Facilitation and Ca2+-dependent inactivation are modified by mutation of the Ca(v)1.2 channel IQ motif J. Biol. Chem. 286 2011 26702 26707
    • (2011) J. Biol. Chem. , vol.286 , pp. 26702-26707
    • Poomvanicha, M.1    Wegener, J.W.2    Blaich, A.3    Fischer, S.4    Domes, K.5    Moosmang, S.6    Hofmann, F.7
  • 41
    • 2342513320 scopus 로고    scopus 로고
    • Crystal structures of apocalmodulin and an apocalmodulin/SK potassium channel gating domain complex
    • DOI 10.1016/j.str.2004.03.017, PII S0969212604001121
    • M.A. Schumacher, M. Crum, and M.C. Miller Crystal structures of apocalmodulin and an apocalmodulin/SK potassium channel gating domain complex Structure 12 2004 849 860 (Pubitemid 38595773)
    • (2004) Structure , vol.12 , Issue.5 , pp. 849-860
    • Schumacher, M.A.1    Crum, M.2    Miller, M.C.3
  • 46
    • 17144415220 scopus 로고    scopus 로고
    • Compendium of cardiac channel mutations in 541 consecutive unrelated patients referred for long QT syndrome genetic testing
    • DOI 10.1016/j.hrthm.2005.01.020, PII S1547527105001918
    • D.J. Tester, M.L. Will, C.M. Haglund, and M.J. Ackerman Compendium of cardiac channel mutations in 541 consecutive unrelated patients referred for long QT syndrome genetic testing Heart Rhythm 2 2005 507 517 (Pubitemid 40521365)
    • (2005) Heart Rhythm , vol.2 , Issue.5 , pp. 507-517
    • Tester, D.J.1    Will, M.L.2    Haglund, C.M.3    Ackerman, M.J.4
  • 50
    • 79959897196 scopus 로고    scopus 로고
    • Identification of novel interaction sites that determine specificity between fibroblast growth factor homologous factors and voltage-gated sodium channels
    • C. Wang, C. Wang, E.G. Hoch, and G.S. Pitt Identification of novel interaction sites that determine specificity between fibroblast growth factor homologous factors and voltage-gated sodium channels J. Biol. Chem. 286 2011 24253 24263
    • (2011) J. Biol. Chem. , vol.286 , pp. 24253-24263
    • Wang, C.1    Wang, C.2    Hoch, E.G.3    Pitt, G.S.4
  • 51
    • 39749151626 scopus 로고    scopus 로고
    • 2+-dependent inactivation of NMDA receptors by dimerizing the NR1 C termini
    • DOI 10.1523/JNEUROSCI.5417-07.2008
    • C. Wang, H.-G. Wang, H. Xie, and G.S. Pitt Ca2+/CaM controls Ca2+-dependent inactivation of NMDA receptors by dimerizing the NR1 C termini J. Neurosci. 28 2008 1865 1870 (Pubitemid 351302664)
    • (2008) Journal of Neuroscience , vol.28 , Issue.8 , pp. 1865-1870
    • Wang, C.1    Wang, H.-G.2    Xie, H.3    Pitt, G.S.4
  • 52
    • 34548152597 scopus 로고    scopus 로고
    • 2+ channels in cultured hippocampal neurons
    • DOI 10.1523/JNEUROSCI.1720-07.2007
    • H.G. Wang, M.S. George, J. Kim, C. Wang, and G.S. Pitt Ca2+/calmodulin regulates trafficking of Ca(V)1.2 Ca2+ channels in cultured hippocampal neurons J. Neurosci. 27 2007 9086 9093 (Pubitemid 47312052)
    • (2007) Journal of Neuroscience , vol.27 , Issue.34 , pp. 9086-9093
    • Wang, H.-G.1    George, M.S.2    Kim, J.3    Wang, C.4    Pitt, G.S.5
  • 55
    • 61849156873 scopus 로고    scopus 로고
    • SCN5A channelopathies - An update on mutations and mechanisms
    • T. Zimmer, and R. Surber SCN5A channelopathies - an update on mutations and mechanisms Prog. Biophys. Mol. Biol. 98 2008 120 136
    • (2008) Prog. Biophys. Mol. Biol. , vol.98 , pp. 120-136
    • Zimmer, T.1    Surber, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.