메뉴 건너뛰기




Volumn 289, Issue 1, 2014, Pages 143-151

Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALS; X RAY CRYSTALLOGRAPHY;

EID: 84891674459     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.501833     Document Type: Article
Times cited : (16)

References (40)
  • 1
    • 77953714921 scopus 로고    scopus 로고
    • Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels
    • Clarke, O. B., Caputo, A. T., Hill, A. P., Vandenberg, J. I., Smith, B. J., and Gulbis, J. M. (2010) Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels. Cell 141, 1018-1029
    • (2010) Cell , vol.141 , pp. 1018-1029
    • Clarke, O.B.1    Caputo, A.T.2    Hill, A.P.3    Vandenberg, J.I.4    Smith, B.J.5    Gulbis, J.M.6
  • 4
    • 84863032002 scopus 로고    scopus 로고
    • Structural rearrangements underlying ligand-gating in Kir channels
    • Wang, S., Lee, S. J., Heyman, S., Enkvetchakul, D., and Nichols, C. G. (2012) Structural rearrangements underlying ligand-gating in Kir channels. Nat Commun. 3, 617
    • (2012) Nat Commun. , vol.3 , pp. 617
    • Wang, S.1    Lee, S.J.2    Heyman, S.3    Enkvetchakul, D.4    Nichols, C.G.5
  • 5
    • 84878996278 scopus 로고    scopus 로고
    • X-ray structure of the mammalian GIRK2-/37 G-protein complex
    • Whorton, M. R., and MacKinnon, R. (2013) X-ray structure of the mammalian GIRK2-/37 G-protein complex. Nature 498, 190-197
    • (2013) Nature , vol.498 , pp. 190-197
    • Whorton, M.R.1    MacKinnon, R.2
  • 10
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • DOI 10.1006/jmbi.1993.1626
    • Sali, A., and Blundell, T. L. (1993) Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815 (Pubitemid 24007801)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 11
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • DOI 10.1093/nar/gkh381
    • Dolinsky, T. J., Nielsen, J. E., McCammon, J. A., and Baker, N. A. (2004) PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res. 32, W665-W667 (Pubitemid 38997419)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISS.
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 12
    • 32844457567 scopus 로고
    • Accurate calculation of hydration free energies using macroscopic solvent models
    • Sitkoff, D., Sharp, K. A., and Honig, B. (1994) Accurate calculation of hydration free energies using macroscopic solvent models. J. Phys. Chem. B 98, 1978-1988
    • (1994) J. Phys. Chem. B , vol.98 , pp. 1978-1988
    • Sitkoff, D.1    Sharp, K.A.2    Honig, B.3
  • 16
    • 79954524314 scopus 로고    scopus 로고
    • From coarse grained to atomistic: A serial multiscale approach to membrane protein simulations
    • Stansfeld, P. J., and Sansom, M. S. P. (2011) From coarse grained to atomistic: a serial multiscale approach to membrane protein simulations. Chem. Theory Comput. 7, 1157-1166
    • (2011) Chem. Theory Comput. , vol.7 , pp. 1157-1166
    • Stansfeld, P.J.1    Sansom, M.S.P.2
  • 17
    • 0035498860 scopus 로고    scopus 로고
    • Energetics of ion conduction through the K+ channel
    • DOI 10.1038/35102067
    • Bernche, S., and Roux, B. (2001) Energetics of ion conduction through the K è channel. Nature 414, 73-77 (Pubitemid 33041625)
    • (2001) Nature , vol.414 , Issue.6859 , pp. 73-77
    • Berneche, S.1    Roux, B.2
  • 18
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • DOI 10.1107/S0907444993011333
    • Kleywegt, G. J., and Jones, T. A. (1994) Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallogr. DBiol. Crystallogr. 50, 178-185 (Pubitemid 2054290)
    • (1994) Acta Crystallographica Section D: Biological Crystallography , vol.50 , Issue.2 , pp. 178-185
    • Kleywegt, G.J.1    Alwyn Jones, T.2
  • 20
    • 80053131218 scopus 로고    scopus 로고
    • Structural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2
    • Hansen, S. B., Tao, X., and MacKinnon, R. (2011) Structural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2. Nature 477, 495-498
    • (2011) Nature , vol.477 , pp. 495-498
    • Hansen, S.B.1    Tao, X.2    MacKinnon, R.3
  • 21
    • 71449120188 scopus 로고    scopus 로고
    • Physical determinants of strong voltage sensitivity of K+ channel block
    • Xu, Y., Shin, H. G., Szép, S., and Lu, Z. (2009) Physical determinants of strong voltage sensitivity of K+ channel block. Nat. Struct. Mol. Biol. 16, 1252-1258
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1252-1258
    • Xu, Y.1    Shin, H.G.2    Szép, S.3    Lu, Z.4
  • 22
    • 64549098161 scopus 로고    scopus 로고
    • KirBac1.1: It's an inward rectifying potassium channel
    • Cheng, W. W., Enkvetchakul, D., and Nichols, C. G. (2009) KirBac1.1: it's an inward rectifying potassium channel. J. Gen. Physiol. 133, 295-305
    • (2009) J. Gen. Physiol. , vol.133 , pp. 295-305
    • Cheng, W.W.1    Enkvetchakul, D.2    Nichols, C.G.3
  • 23
    • 0029025529 scopus 로고
    • Control of rectification and permeation by residues in two distinct domains in an inward rectifier K+ channel
    • Yang, J., Jan, Y. N, and Jan, L. Y. (1995) Control of rectification and permeation by residues in two distinct domains in an inward rectifier K + channel. Neuron 14, 1047-1054
    • (1995) Neuron , vol.14 , pp. 1047-1054
    • Yang, J.1    Jan, Y.N.2    Jan, L.Y.3
  • 24
    • 82355181506 scopus 로고    scopus 로고
    • Interactions of cations with the cytoplasmic pores of inward rectifier K+ channels in the closed state
    • Inanobe, A., Nakagawa, A., and Kurachi, Y. (2011) Interactions of cations with the cytoplasmic pores of inward rectifier K+ channels in the closed state. J. Biol. Chem. 286, 41801-41811
    • (2011) J. Biol. Chem. , vol.286 , pp. 41801-41811
    • Inanobe, A.1    Nakagawa, A.2    Kurachi, Y.3
  • 25
    • 34547621771 scopus 로고    scopus 로고
    • The role of the cytoplasmic pore in inward rectification of Kir2.1 channels
    • DOI 10.1085/jgp.200709742
    • Kurata, H. T., Cheng, W. W., Arrabit, C., Slesinger, P. A., and Nichols, C. G. (2007) The role of the cytoplasmic pore in inward rectification of Kir2.1 channels. J. Gen. Physiol. 130, 145-155 (Pubitemid 47204906)
    • (2007) Journal of General Physiology , vol.130 , Issue.2 , pp. 145-155
    • Kurata, H.T.1    Cheng, W.W.2    Arrabit, C.3    Slesinger, P.A.4    Nichols, C.G.5
  • 26
    • 14544298750 scopus 로고    scopus 로고
    • Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification
    • DOI 10.1038/nn1411
    • Pegan, S., Arrabit, C., Zhou, W., Kwiatkowski, W., Collins, A., Slesinger, P. A., and Choe, S. (2005) Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification. Nat. Neurosci. 8, 279-287 (Pubitemid 40300184)
    • (2005) Nature Neuroscience , vol.8 , Issue.3 , pp. 279-287
    • Pegan, S.1    Arrabit, C.2    Zhou, W.3    Kwiatkowski, W.4    Collins, A.5    Slesinger, P.A.6    Choe, S.7
  • 27
    • 33645325379 scopus 로고    scopus 로고
    • Functional roles of charged amino acid residues on the wall of the cytoplasmic pore of Kir2.1
    • Fujiwara, Y., and Kubo, Y. (2006) Functional roles of charged amino acid residues on the wall of the cytoplasmic pore of Kir2.1. J. Gen. Physiol. 127, 401-419
    • (2006) J. Gen. Physiol. , vol.127 , pp. 401-419
    • Fujiwara, Y.1    Kubo, Y.2
  • 28
    • 11244348916 scopus 로고    scopus 로고
    • A ring of negative charges in the intracellular vestibule of Kir2.1 channel modulates K+ permeation
    • Chang, H. K., Yeh, S. H., and Shieh, R. C. (2005) A ring of negative charges in the intracellular vestibule of Kir2.1 channel modulates K+ permeation. Biophys. J. 88, 243-254
    • (2005) Biophys. J. , vol.88 , pp. 243-254
    • Chang, H.K.1    Yeh, S.H.2    Shieh, R.C.3
  • 29
    • 33746047139 scopus 로고    scopus 로고
    • Andersen's syndrome mutation effects on the structure and assembly of the cytoplasmic domains of Kir2.1
    • DOI 10.1021/bi060653d
    • Pegan, S., Arrabit, C., Slesinger, P. A., and Choe, S. (2006) Andersen's syndrome mutation effects on the structure and assembly of the cytoplasmic domains of Kir2.1. Biochemistry 45, 8599-8606 (Pubitemid 44078880)
    • (2006) Biochemistry , vol.45 , Issue.28 , pp. 8599-8606
    • Pegan, S.1    Arrabit, C.2    Slesinger, P.A.3    Choe, S.4
  • 31
    • 34548049980 scopus 로고    scopus 로고
    • Charges in the cytoplasmic pore control intrinsic inward rectification and single-channel properties in Kir1.1 and Kir2.1 channels
    • Chang, H. K., Yeh, S. H., and Shieh, R. C. (2007) Charges in the cytoplasmic pore control intrinsic inward rectification and single-channel properties in Kir1.1 and Kir2.1 channels. J. Membr. Biol. 215, 181-193
    • (2007) J. Membr. Biol. , vol.215 , pp. 181-193
    • Chang, H.K.1    Yeh, S.H.2    Shieh, R.C.3
  • 32
    • 0033557704 scopus 로고    scopus 로고
    • Inward rectification in K(ATP) channels: A pH switch in the pore
    • DOI 10.1093/emboj/18.4.847
    • Baukrowitz, T., Tucker, S. J., Schulte, U., Benndorf, K., Ruppersberg, J. P., and Fakler, B. (1999) Inward rectification in KATP channels: a pH switch in the pore. EMBO J. 18, 847-853 (Pubitemid 29082264)
    • (1999) EMBO Journal , vol.18 , Issue.4 , pp. 847-853
    • Baukrowitz, T.1    Tucker, S.J.2    Schulte, U.3    Benndorf, K.4    Ruppersberg, J.P.5    Fakler, B.6
  • 33
    • 0033754410 scopus 로고    scopus 로고
    • A single residue contributes to the difference between Kir4.1 and Kir1.1 channels in pH sensitivity, rectification and single channel conductance
    • Xu, H., Yang, Z., Cui, N., Chanchevalap, S., Valesky, W. W., and Jiang, C. (2000) A single residue contributes to the difference between Kir4.1 and Kir1.1 channels in pH sensitivity, rectification and single channel conductance. J. Physiol. 528, 267-277
    • (2000) J. Physiol. , vol.528 , pp. 267-277
    • Xu, H.1    Yang, Z.2    Cui, N.3    Chanchevalap, S.4    Valesky, W.W.5    Jiang, C.6
  • 34
    • 0242290267 scopus 로고    scopus 로고
    • Identification of a Heteromeric Interaction that Influences the Rectification, Gating, and pH Sensitivity of Kir4.1/Kir5.1 Potassium Channels
    • DOI 10.1074/jbc.M306596200
    • Casamassima, M., D'Adamo, M. C., Pessia, M., and Tucker, S. J. (2003) Identification of a heteromeric interaction that influences the rectification, gating, and pH sensitivity of Kir4.1/Kir5.1 potassium channels. J. Biol. Chem. 278, 43533-43540 (Pubitemid 37345977)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.44 , pp. 43533-43540
    • Casamassima, M.1    D'Adamo, M.C.2    Pessia, M.3    Tucker, S.J.4
  • 35
    • 34547683445 scopus 로고    scopus 로고
    • H Bonding at the helix-bundle crossing controls gating in kir potassium channels
    • DOI 10.1016/j.neuron.2007.07.026, PII S0896627307005715
    • Rapedius, M., Fowler, P. W., Shang, L., Sansom, M. S., Tucker, S. J., and Baukrowitz, T. (2007) H bonding at the helix-bundle crossing controls gating in Kir potassium channels. Neuron 55, 602-614 (Pubitemid 47223642)
    • (2007) Neuron , vol.55 , Issue.4 , pp. 602-614
    • Rapedius, M.1    Fowler, P.W.2    Shang, L.3    Sansom, M.S.P.4    Tucker, S.J.5    Baukrowitz, T.6
  • 36
    • 77957724718 scopus 로고    scopus 로고
    • Random mutagenesis screening indicates the absence of a separate H+-sensor in the pH-sensitive Kir channels
    • Paynter, J. J., Shang, L., Bollepalli, M. K., Baukrowitz, T., and Tucker, S. J. (2010) Random mutagenesis screening indicates the absence of a separate H+-sensor in the pH-sensitive Kir channels. Channels 4, 390-397
    • (2010) Channels , vol.4 , pp. 390-397
    • Paynter, J.J.1    Shang, L.2    Bollepalli, M.K.3    Baukrowitz, T.4    Tucker, S.J.5
  • 39
    • 84859963646 scopus 로고    scopus 로고
    • Mutations that stabilize the open state of the Erwinia chrisanthemi ligand-gated ion channel fail to change the conformation of the pore domain in crystals
    • Gonzalez-Gutierrez, G., Lukk, T., Agarwal, V., Papke, D., Nair, S. K., and Grosman, C. (2012) Mutations that stabilize the open state of the Erwinia chrisanthemi ligand-gated ion channel fail to change the conformation of the pore domain in crystals. Proc. Natl. Acad. Sci. U. S. A. 109, 6331-6336
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 6331-6336
    • Gonzalez-Gutierrez, G.1    Lukk, T.2    Agarwal, V.3    Papke, D.4    Nair, S.K.5    Grosman, C.6
  • 40
    • 0030404988 scopus 로고    scopus 로고
    • HOLE: A program for the analysis of the pore dimensions of ion channel structural models
    • DOI 10.1016/S0263-7855(97)00009-X, PII S026378559700009X
    • Smart, O. S., Neduvelil, J. G., Wang, X., Wallace, B. A., and Sansom, M. S. (1996) HOLE: a program for the analysis of the pore dimensions of ion channel structural models. J. Mol. Graph. 14, 354-360 (Pubitemid 27302826)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.6 , pp. 354-360
    • Smart, O.S.1    Neduvelil, J.G.2    Wang, X.3    Wallace, B.A.4    Sansom, M.S.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.