메뉴 건너뛰기




Volumn 461, Issue 1, 2011, Pages 53-63

Physicochemical properties of pore residues predict activation gating of CaV1.2: A correlation mutation analysis

Author keywords

Activation determinants; Amino acid descriptors; Calcium channels; Pore stability

Indexed keywords

ALANINE; ASPARAGINE; BARIUM ION; CALCIUM CHANNEL CAV1.2; GLUTAMINE; GLYCINE; LEUCINE; METHIONINE; PROLINE; THREONINE; TRYPTOPHAN; UNCLASSIFIED DRUG; VALINE; VOLTAGE GATED CALCIUM CHANNEL;

EID: 78751643127     PISSN: 00316768     EISSN: 14322013     Source Type: Journal    
DOI: 10.1007/s00424-010-0885-2     Document Type: Article
Times cited : (7)

References (36)
  • 1
    • 0142215620 scopus 로고    scopus 로고
    • Cardiac calcium signalling
    • 1:CAS:528:DC%2BD3sXnsVyjsbg%3D 10.1042/BST0310930 14505451
    • MJ Berridge 2003 Cardiac calcium signalling Biochem Soc Trans 31 930 933 1:CAS:528:DC%2BD3sXnsVyjsbg%3D 10.1042/BST0310930 14505451
    • (2003) Biochem Soc Trans , vol.31 , pp. 930-933
    • Berridge, M.J.1
  • 2
    • 69749115277 scopus 로고    scopus 로고
    • Different pathways for activation and deactivation in CaV1.2: A minimal gating model
    • 1:CAS:528:DC%2BD1MXhtF2jsLbO 10.1085/jgp.200910272 19687230
    • S Beyl P Kügler M Kudrnac A Hohaus S Hering E Timin 2009 Different pathways for activation and deactivation in CaV1.2: a minimal gating model J Gen Physiol 134 231 241 1:CAS:528:DC%2BD1MXhtF2jsLbO 10.1085/jgp.200910272 19687230
    • (2009) J Gen Physiol , vol.134 , pp. 231-241
    • Beyl, S.1    Kügler, P.2    Kudrnac, M.3    Hohaus, A.4    Hering, S.5    Timin, E.6
  • 3
    • 33947532545 scopus 로고    scopus 로고
    • Probing the architecture of an L-type calcium channel with a charged phenylalkylamine: Evidence for a widely open pore and drug trapping
    • DOI 10.1074/jbc.M609153200
    • S Beyl EN Timin A Hohaus A Stary M Kudrnac RH Guy S Hering 2007 Probing the architecture of an L-type calcium channel with a charged phenylalkylamine: evidence for a widely open pore and drug trapping J Biol Chem 282 3864 3870 1:CAS:528:DC%2BD2sXht1KqtbY%3D 10.1074/jbc.M609153200 17138559 (Pubitemid 47084465)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.6 , pp. 3864-3870
    • Beyl, S.1    Timin, E.N.2    Hohaus, A.3    Stary, A.4    Kudrnac, M.5    Guy, R.H.6    Hering, S.7
  • 4
    • 0027236794 scopus 로고
    • Structural basis of amino acid alpha helix propensity
    • 1:CAS:528:DyaK3sXks1KjsL0%3D 10.1126/science.8503008 8503008
    • M Blaber XJ Zhang BW Matthews 1993 Structural basis of amino acid alpha helix propensity Science 260 1637 1640 1:CAS:528:DyaK3sXks1KjsL0%3D 10.1126/science.8503008 8503008
    • (1993) Science , vol.260 , pp. 1637-1640
    • Blaber, M.1    Zhang, X.J.2    Matthews, B.W.3
  • 5
    • 0031956790 scopus 로고    scopus 로고
    • The dimerization motif of the glycophorin A transmembrane segment in membranes: Importance of glycine residues
    • 1:CAS:528:DyaK1cXisFSnu7Y%3D 10.1002/pro.5560070423 9568912
    • B Brosig D Langosch 1998 The dimerization motif of the glycophorin A transmembrane segment in membranes: importance of glycine residues Protein Sci 7 1052 1056 1:CAS:528:DyaK1cXisFSnu7Y%3D 10.1002/pro.5560070423 9568912
    • (1998) Protein Sci , vol.7 , pp. 1052-1056
    • Brosig, B.1    Langosch, D.2
  • 6
    • 0034518423 scopus 로고    scopus 로고
    • 2+ channels
    • DOI 10.1146/annurev.cellbio.16.1.521
    • WA Catterall 2000 Structure and regulation of voltage-gated Ca2+ channels Annu Rev Cell Dev Biol 16 521 555 1:CAS:528:DC%2BD3MXpvFyr 10.1146/annurev. cellbio.16.1.521 11031246 (Pubitemid 32037516)
    • (2000) Annual Review of Cell and Developmental Biology , vol.16 , pp. 521-555
    • Catterall, W.A.1
  • 7
    • 29844439240 scopus 로고    scopus 로고
    • International Union of Pharmacology. XLVIII. Nomenclature and structure-function relationships of voltage-gated calcium channels
    • DOI 10.1124/pr.57.4.5
    • WA Catterall E Perez-Reyes TP Snutch J Striessnig 2005 International Union of Pharmacology. XLVIII. Nomenclature and structure-function relationships of voltage-gated calcium channels Pharmacol Rev 57 411 425 1:CAS:528: DC%2BD28XhtFWgu7w%3D 10.1124/pr.57.4.5 16382099 (Pubitemid 43036432)
    • (2005) Pharmacological Reviews , vol.57 , Issue.4 , pp. 411-425
    • Catterall, W.A.1    Perez-Reyes, E.2    Snutch, T.P.3    Striessnig, J.4
  • 8
    • 0016352763 scopus 로고
    • Hydrophobic bonding and accessible surface area in proteins
    • 1:CAS:528:DyaE2cXktFSmtr0%3D 10.1038/248338a0 4819639
    • C Chothia 1974 Hydrophobic bonding and accessible surface area in proteins Nature 248 338 339 1:CAS:528:DyaE2cXktFSmtr0%3D 10.1038/248338a0 4819639
    • (1974) Nature , vol.248 , pp. 338-339
    • Chothia, C.1
  • 10
    • 0023753747 scopus 로고
    • Sequence and expression of mRNAs encoding the alpha 1 and alpha 2 subunits of a DHP-sensitive calcium channel
    • 1:CAS:528:DyaL1MXhvVOjsb4%3D 10.1126/science.2458626 2458626
    • SB Ellis ME Williams NR Ways R Brenner AH Sharp AT Leung KP Campbell E McKenna WJ Koch A Hui, et al. 1988 Sequence and expression of mRNAs encoding the alpha 1 and alpha 2 subunits of a DHP-sensitive calcium channel Science 241 1661 1664 1:CAS:528:DyaL1MXhvVOjsb4%3D 10.1126/science.2458626 2458626
    • (1988) Science , vol.241 , pp. 1661-1664
    • Ellis, S.B.1    Williams, M.E.2    Ways, N.R.3    Brenner, R.4    Sharp, A.H.5    Leung, A.T.6    Campbell, K.P.7    McKenna, E.8    Koch, W.J.9    Hui, A.10
  • 11
    • 78650175434 scopus 로고    scopus 로고
    • Extensions to amino acid description
    • 101007/s11030-009-9204-2 19937466
    • J Gottfries L Eriksson 2009 Extensions to amino acid description Mol Divers 101007/s11030-009-9204-2 19937466
    • (2009) Mol Divers
    • Gottfries, J.1    Eriksson, L.2
  • 13
    • 0021977590 scopus 로고
    • Amino acid side-chain partition energies and distribution of residues in soluble proteins
    • 1:CAS:528:DyaL2MXptFKjuw%3D%3D 10.1016/S0006-3495(85)83877-7 3978191
    • HR Guy 1985 Amino acid side-chain partition energies and distribution of residues in soluble proteins Biophys J 47 61 70 1:CAS:528:DyaL2MXptFKjuw%3D%3D 10.1016/S0006-3495(85)83877-7 3978191
    • (1985) Biophys J , vol.47 , pp. 61-70
    • Guy, H.R.1
  • 14
    • 0036016539 scopus 로고    scopus 로고
    • Scanning the intracellular S6 activation gate in the shaker K+ channel
    • DOI 10.1085/jgp.20028569
    • DH Hackos TH Chang KJ Swartz 2002 Scanning the intracellular S6 activation gate in the shaker K+ channel J Gen Physiol 119 521 532 1:CAS:528:DC%2BD38XltVSmt7g%3D 10.1085/jgp.20028569 12034760 (Pubitemid 34615097)
    • (2002) Journal of General Physiology , vol.119 , Issue.6 , pp. 521-531
    • Hackos, D.H.1    Chang, T.-H.2    Swartz, K.J.3
  • 15
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • DOI 10.1007/BF00656997
    • OP Hamill A Marty E Neher B Sakmann FJ Sigworth 1981 Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches Pflugers Arch 391 85 100 1:STN:280:DyaL38%2FjslWrug%3D%3D 10.1007/BF00656997 6270629 (Pubitemid 11012976)
    • (1981) Pflugers Archiv European Journal of Physiology , vol.391 , Issue.2 , pp. 85-100
    • Hamill, O.P.1    Marty, A.2    Neher, E.3
  • 17
    • 67649739370 scopus 로고    scopus 로고
    • Pore stability and gating in voltage-activated calcium channels
    • 10.4161/chan.2.2.5999 18849656
    • S Hering S Beyl A Stary M Kudrnac A Hohaus HR Guy E Timin 2008 Pore stability and gating in voltage-activated calcium channels Channels 2 61 69 10.4161/chan.2.2.5999 18849656
    • (2008) Channels , vol.2 , pp. 61-69
    • Hering, S.1    Beyl, S.2    Stary, A.3    Kudrnac, M.4    Hohaus, A.5    Guy, H.R.6    Timin, E.7
  • 18
    • 13444262028 scopus 로고    scopus 로고
    • Recognition of transmembrane helices by the endoplasmic reticulum translocon
    • DOI 10.1038/nature03216
    • T Hessa H Kim K Bihlmaier C Lundin J Boekel H Ersson I Nilsson SH White G von Heijne 2005 Recognition of transmembrane helices by the endoplasmic reticulum translocon Nature 433 377 381 1:CAS:528:DC%2BD2MXnt1Wjug%3D%3D 10.1038/nature03216 15674282 (Pubitemid 40203311)
    • (2005) Nature , vol.433 , Issue.7024 , pp. 377-381
    • Hessa, T.1    Kim, H.2    Bihlmaier, K.3    Lundin, C.4    Boekel, J.5    Andersson, H.6    Nilsson, I.7    White, S.H.8    Von Heijne, G.9
  • 19
    • 33644684859 scopus 로고    scopus 로고
    • Structural determinants of L-type channel activation in segment IIS6 revealed by a retinal disorder
    • DOI 10.1074/jbc.M507013200
    • A Hohaus S Beyl M Kudrnac S Berjukow EN Timin R Marksteiner MA Maw S Hering 2005 Structural determinants of L-type channel activation in segment IIS6 revealed by a retinal disorder J Biol Chem 280 38471 38477 1:CAS:528: DC%2BD2MXht1SktL3L 10.1074/jbc.M507013200 16157588 (Pubitemid 43853745)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.46 , pp. 38471-38477
    • Hohaus, A.1    Beyl, S.2    Kudrnac, M.3    Berjukow, S.4    Timin, E.N.5    Marksteiner, R.6    Maw, M.A.7    Hering, S.8
  • 21
    • 0037198625 scopus 로고    scopus 로고
    • The open pore conformation of potassium channels
    • DOI 10.1038/417523a
    • Y Jiang A Lee J Chen M Cadene BT Chait R MacKinnon 2002 The open pore conformation of potassium channels Nature 417 523 526 1:CAS:528: DC%2BD38XktVeht7k%3D 10.1038/417523a 12037560 (Pubitemid 34595913)
    • (2002) Nature , vol.417 , Issue.6888 , pp. 523-526
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 22
    • 66449097492 scopus 로고    scopus 로고
    • Coupled and independent contributions of residues in IS6 and IIS6 to activation gating of CaV1.2
    • 1:CAS:528:DC%2BD1MXltVCmu7k%3D 10.1074/jbc.M808402200 19265197
    • M Kudrnac S Beyl A Hohaus A Stary T Peterbauer E Timin S Hering 2009 Coupled and independent contributions of residues in IS6 and IIS6 to activation gating of CaV1.2 J Biol Chem 284 12276 12284 1:CAS:528:DC%2BD1MXltVCmu7k%3D 10.1074/jbc.M808402200 19265197
    • (2009) J Biol Chem , vol.284 , pp. 12276-12284
    • Kudrnac, M.1    Beyl, S.2    Hohaus, A.3    Stary, A.4    Peterbauer, T.5    Timin, E.6    Hering, S.7
  • 23
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • 1:CAS:528:DyaL38Xks1yjtro%3D 10.1016/0022-2836(82)90515-0 7108955
    • J Kyte RF Doolittle 1982 A simple method for displaying the hydropathic character of a protein J Mol Biol 157 105 132 1:CAS:528:DyaL38Xks1yjtro%3D 10.1016/0022-2836(82)90515-0 7108955
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 24
    • 6344285843 scopus 로고    scopus 로고
    • Conserved gating hinge in ligand- and voltage-dependent K+ channels
    • 1:CAS:528:DC%2BD2cXotVCjtrk%3D 10.1021/bi048377v 15491131
    • E Magidovich O Yifrach 2004 Conserved gating hinge in ligand- and voltage-dependent K+ channels Biochemistry 43 13242 13247 1:CAS:528: DC%2BD2cXotVCjtrk%3D 10.1021/bi048377v 15491131
    • (2004) Biochemistry , vol.43 , pp. 13242-13247
    • Magidovich, E.1    Yifrach, O.2
  • 25
    • 0033527670 scopus 로고    scopus 로고
    • Turns in transmembrane helices: Determination of the minimal length of a 'Helical hairpin' and derivation of a fine-grained turn propensity scale
    • DOI 10.1006/jmbi.1999.3183
    • M Monné I Nilsson A Elofsson G von Heijne 1999 Turns in transmembrane helices: determination of the minimal length of a "helical hairpin" and derivation of a fine-grained turn propensity scale J Mol Biol 293 807 814 10.1006/jmbi.1999.3183 10543969 (Pubitemid 29527668)
    • (1999) Journal of Molecular Biology , vol.293 , Issue.4 , pp. 807-814
    • Monne, M.1    Nilsson, I.2    Elofsson, A.3    Von Heijne, G.4
  • 29
    • 0022412192 scopus 로고
    • Hydrophobicity of amino acid residues in globular proteins
    • 1:CAS:528:DyaL2MXlslChs7g%3D 10.1126/science.4023714 4023714
    • GD Rose AR Geselowitz GJ Lesser RH Lee MH Zehfus 1985 Hydrophobicity of amino acid residues in globular proteins Science 229 834 838 1:CAS:528:DyaL2MXlslChs7g%3D 10.1126/science.4023714 4023714
    • (1985) Science , vol.229 , pp. 834-838
    • Rose, G.D.1    Geselowitz, A.R.2    Lesser, G.J.3    Lee, R.H.4    Zehfus, M.H.5
  • 30
    • 38049148291 scopus 로고    scopus 로고
    • Principles underlying energetic coupling along an allosteric communication trajectory of a voltage-activated K+ channel
    • 1:CAS:528:DC%2BD1cXitFSrtw%3D%3D 10.1073/pnas.0708120104 18077413
    • E Sadovsky O Yifrach 2007 Principles underlying energetic coupling along an allosteric communication trajectory of a voltage-activated K+ channel Proc Natl Acad Sci U S A 104 19813 19818 1:CAS:528:DC%2BD1cXitFSrtw%3D%3D 10.1073/pnas.0708120104 18077413
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 19813-19818
    • Sadovsky, E.1    Yifrach, O.2
  • 31
    • 0026076664 scopus 로고
    • Extracting hydrophobic free energies from experimental data: Relationship to protein folding and theoretical models
    • 1:CAS:528:DyaK3MXlslyrsrY%3D 10.1021/bi00104a017 1911756
    • KA Sharp A Nicholls R Friedman B Honig 1991 Extracting hydrophobic free energies from experimental data: relationship to protein folding and theoretical models Biochemistry 30 9686 9697 1:CAS:528:DyaK3MXlslyrsrY%3D 10.1021/bi00104a017 1911756
    • (1991) Biochemistry , vol.30 , pp. 9686-9697
    • Sharp, K.A.1    Nicholls, A.2    Friedman, R.3    Honig, B.4
  • 32
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • DOI 10.1146/annurev.biophys.28.1.319
    • SH White WC Wimley 1999 Membrane protein folding and stability: physical principles Annu Rev Biophys Biomol Struct 28 319 365 1:CAS:528: DyaK1MXkt1erurs%3D 10.1146/annurev.biophys.28.1.319 10410805 (Pubitemid 29319262)
    • (1999) Annual Review of Biophysics and Biomolecular Structure , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 33
    • 0037131520 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1016/S0092-8674(02)01013-9
    • O Yifrach R MacKinnon 2002 Energetics of pore opening in a voltage-gated K(+) channel Cell 111 231 239 1:CAS:528:DC%2BD38Xotlahsrs%3D 10.1016/S0092-8674(02)01013-9 12408867 (Pubitemid 35292443)
    • (2002) Cell , vol.111 , Issue.2 , pp. 231-239
    • Yifrach, O.1    MacKinnon, R.2
  • 34
    • 11144221751 scopus 로고    scopus 로고
    • Reversed voltage-dependent gating of a bacterial sodium channel with proline substitutions in the S6 transmembrane segment
    • DOI 10.1073/pnas.0408270101
    • Y Zhao T Scheuer WA Catterall 2004 Reversed voltage-dependent gating of a bacterial sodium channel with proline substitutions in the S6 transmembrane segment Proc Natl Acad Sci U S A 101 17873 17878 1:CAS:528: DC%2BD2MXjtVSlsg%3D%3D 10.1073/pnas.0408270101 15583130 (Pubitemid 40051979)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.51 , pp. 17873-17878
    • Zhao, Y.1    Scheuer, T.2    Catterall, W.A.3
  • 35
    • 1842422868 scopus 로고    scopus 로고
    • + channels: A molecular switch for electrical signaling
    • DOI 10.1016/S0896-6273(04)00116-3, PII S0896627304001163
    • Y Zhao V Yarov-Yarovoy T Scheuer WA Catterall 2004 A gating hinge in Na+ channels; a molecular switch for electrical signaling Neuron 41 859 865 1:CAS:528:DC%2BD2cXjtValtLw%3D 10.1016/S0896-6273(04)00116-3 15046719 (Pubitemid 38429730)
    • (2004) Neuron , vol.41 , Issue.6 , pp. 859-865
    • Zhao, Y.1    Yarov-Yarovoy, V.2    Scheuer, T.3    Catterall, W.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.