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Science 14 April 1995:
Vol. 268. no. 5208, pp. 307 - 310
DOI: 10.1126/science.7716527
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Articles

Science, Vol 268, Issue 5208, 307-310
Copyright © 1995 by American Association for the Advancement of Science

articles

Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor

P Hidalgo and R MacKinnon

Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.

Thermodynamic mutant cycles provide a formalism for studying energetic coupling between amino acids on the interaction surface in a protein-protein complex. This approach was applied to the Shaker potassium channel and to a high-affinity peptide inhibitor (scorpion toxin) that binds to its pore entryway. The assignment of pairwise interactions defined the spatial arrangement of channel amino acids with respect to the known inhibitor structure. A strong constraint was placed on the Shaker channel pore-forming region by requiring its amino-terminal border to be 12 to 15 angstroms from the central axis. This method is directly applicable to sodium, calcium, and other ion channels where inhibitor or modulatory proteins bind with high affinity.


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Pairwise Interactions between Neuronal alpha 7 Acetylcholine Receptors and alpha -Conotoxin ImI.
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Sequence of Events Underlying the Allosteric Transition of Rod Cyclic Nucleotide-gated Channels.
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Analysis of protein–protein interactions by mutagenesis: direct versus indirect effects.
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C Dart, M L Leyland, P J Spencer, P R Stanfield, and M J Sutcliffe (1998)
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Mutations at Lipid-Exposed Residues of the Acetylcholine Receptor Affect Its Gating Kinetics.
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D. A. Doyle, J. M. Cabral, R. A. Pfuetzner, A. Kuo, J. M. Gulbis, S. L. Cohen, B. T. Chait, and R. MacKinnon (1998)
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Structural Conservation in Prokaryotic and Eukaryotic Potassium Channels.
R. MacKinnon, S. L. Cohen, A. Kuo, A. Lee, and B. T. Chait (1998)
Science 280, 106-109
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Specific Antibodies to the External Vestibule of Voltage-gated Potassium Channels Block Current.
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J. Gen. Physiol. 111, 555-563
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Sea Anemone Peptides with a Specific Blocking Activity against the Fast Inactivating Potassium Channel Kv3.4.
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Proton Probing of the Charybdotoxin Binding Site of Shaker K+ Channels.
P. Perez-Cornejo, P. Stampe, and T. Begenisich (1998)
J. Gen. Physiol. 111, 441-450
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The Interaction of Na+ and K+ in Voltage-gated Potassium Channels: Evidence for Cation Binding Sites of Different Affinity.
L. Kiss, D. Immke, J. LoTurco, and S. J. Korn (1998)
J. Gen. Physiol. 111, 195-206
   Abstract »    Full Text »    PDF »
Regulation of mammalian Shaker-related K+ channels: evidence for non-conducting closed and non-conducting inactivated states.
H. Jager, H. Rauer, A. N Nguyen, J. Aiyar, K G. Chandy, and S. Grissmer (1998)
J. Physiol. 506, 291-301
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A Specific Interaction between the Cardiac Sodium Channel and Site-3 Toxin Anthopleurin B.
G. R. Benzinger, J. W. Kyle, K. M. Blumenthal, and D. A. Hanck (1998)
J. Biol. Chem. 273, 80-84
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The Functional Architecture of an Acetylcholine Receptor-mimicking Antibody.
K. Merienne, N. Germain, S. Zinn-Justin, J.-C. Boulain, F. Ducancel, and A. Menez (1997)
J. Biol. Chem. 272, 23775-23783
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P-loop Flexibility in Na+ Channel Pores Revealed by Single- and Double-cysteine Replacements.
R. G. Tsushima, R. A. Li, and P. H. Backx (1997)
J. Gen. Physiol. 110, 59-72
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Preferential Interaction of omega -Conotoxins with Inactivated N-type Ca2+ Channels.
J. W. Stocker, L. Nadasdi, R. W. Aldrich, and R. W. Tsien (1997)
J. Neurosci. 17, 3002-3013
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Separation of Gating Properties from Permeation and Block in mslo Large Conductance Ca-activated K+ Channels.
D.H. Cox, J. Cui, and R.W. Aldrich (1997)
J. Gen. Physiol. 109, 633-646
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Stabilization of ion selectivity filter by pore loop ion pairs in an inwardly rectifying potassium channel.
J. Yang, M. Yu, Y. N. Jan, and L. Y. Jan (1997)
PNAS 94, 1568-1572
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Purification, Visualization, and Biophysical Characterization of Kv1.3 Tetramers.
R. H. Spencer, Y. Sokolov, H. Li, B. Takenaka, A. J. Milici, J. Aiyar, A. Nguyen, H. Park, B. K. Jap, J. E. Hall, et al. (1997)
J. Biol. Chem. 272, 2389-2395
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The Signature Sequence of Voltage-gated Potassium Channels Projects into the External Vestibule.
J. Aiyar, J. P. Rizzi, G. A. Gutman, and K. G. Chandy (1996)
J. Biol. Chem. 271, 31013-31016
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Silver as a probe of pore-forming residues in a potassium channel.
Q Lu and C Miller (1995)
Science 268, 304-307
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R. B. Jacobsen, E. D. Koch, B. Lange-Malecki, M. Stocker, J. Verhey, R. M. Van Wagoner, A. Vyazovkina, B. M. Olivera, and H. Terlau (2000)
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   Abstract »    Full Text »    PDF »
An ERG Channel Inhibitor from the Scorpion Buthus eupeus.
Y. V. Korolkova, S. A. Kozlov, A. V. Lipkin, K. A. Pluzhnikov, J. K. Hadley, A. K. Filippov, D. A. Brown, K. Angelo, D. Strobak, T. Jespersen, et al. (2001)
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Structural Differences of Bacterial and Mammalian K+ Channels.
A. Wrisch and S. Grissmer (2000)
J. Biol. Chem. 275, 39345-39353
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An Activation Switch in the Ligand Binding Pocket of the C5a Receptor.
B. O. Gerber, E. C. Meng, V. Dotsch, T. J. Baranski, and H. R. Bourne (2001)
J. Biol. Chem. 276, 3394-3400
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Molecular Characterization of Calmodulin Trapping by Calcium/Calmodulin-dependent Protein Kinase II.
S. I. Singla, A. Hudmon, J. M. Goldberg, J. L. Smith, and H. Schulman (2001)
J. Biol. Chem. 276, 29353-29360
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Molecular Determinants by Which a Long Chain Toxin from Snake Venom Interacts with the Neuronal alpha 7-Nicotinic Acetylcholine Receptor.
S. Antil-Delbeke, C. Gaillard, T. Tamiya, P.-J. Corringer, J.-P. Changeux, D. Servent, and A. Menez (2000)
J. Biol. Chem. 275, 29594-29601
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Experimentally based model of a complex between a snake toxin and the alpha 7 nicotinic receptor.
C. Fruchart-Gaillard, B. Gilquin, S. Antil-Delbeke, N. Le Novere, T. Tamiya, P.-J. Corringer, J.-P. Changeux, A. Menez, and D. Servent (2002)
PNAS 99, 3216-3221
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Glycine residues in potassium channel-like selectivity filters determine potassium selectivity in four-loop-per-subunit HKT transporters from plants.
P. Maser, Y. Hosoo, S. Goshima, T. Horie, B. Eckelman, K. Yamada, K. Yoshida, E. P. Bakker, A. Shinmyo, S. Oiki, et al. (2002)
PNAS 99, 6428-6433
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