Spatial localization of the K+ channel selectivity filter by mutant cycle-based structure analysis

Neuron

Volumn 16, Issue 1, 1996, Pages 131-139

  Ranganathan, Rama ^a,b   Lewis, John H ^a   MacKinnon, Roderick ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

POTASSIUM CHANNEL; SCORPION VENOM;

ANIMAL CELL; ARTICLE; CHANNEL GATING; ION PERMEABILITY; NONHUMAN; OOCYTE; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN LOCALIZATION; XENOPUS LAEVIS;

EID: 0030064382     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(00)80030-6     Document Type: Article

References (34)

1. + channel revealed by the NMR-derived structures of scorpion toxins. Neuron 15, 1169-1181.
2. Amit, A.G., Mariuzza, R.A., Phillips, S.E.V., and Poljak, R.J. (1986). Three-dimensional structure of an antigen-antibody complex at 2.8 Å resolution. Science 233, 747-753.
3. + channels. Effects of channel gating, voltage, and ionic strength. J. Gen. Physiol. 91, 317-333.
4. Botems, F., Roumestand, C., Gilquin, B., Menez, A., and Toma, F. (1991). Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins. Science 254, 1521-1523.
5. Carter, P.J., Winter, G., Wilkison, A.J., and Fersht, A.R. (1984). The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus). Cell 38, 835-840.
6. Clackson, T., and Wells, J.A. (1995). A hot spot of binding energy in a hormone-receptor interface. Science 267, 383-386.
7. Davies, D.R., Sheriff, S., and Padlan, E.A. (1988). Antibody-antigen complexes. J. Biol. Chem. 263, 10541-10544.
8. DeVos, A.M., Ultsch, M., and Kossiakoff, A.A. (1992). Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 255, 306-312.
9. Escobar, L., Root, M.J., and MacKinnon, R. (1993). Influence of protein surface charge on the bimolecular kinetics of a potassium channel peptide inhibitor. Biochemistry 32, 6982-6987.
10. + channels from Leiurus Quinquestriatus var. hebraeus venom. Biochemistry 33, 6834-6839.
11. + channel: peptide and channel residues mediating molecular recognition. Neuron 12, 1377-1388.
12. Gross, A., and MacKinnon, R. (1996). Agitoxin footprinting the Shaker potassium channel pore. Neuron, in press.
13. Heginbotham, L., and MacKinnon, R. (1992). The aromatic binding site for tetraethylammonium ion on potassium channels. Neuron 8, 483-491.
14. + channel signature sequence. Biophys. J. 66, 1061-1067.
15. Hidalgo, P. (1995). Obtaining Structural Data of the Pore-Forming Region of the Shaker Potassium Channel using the Scorpion Toxin Agitoxin2 (Santiago, Chile: Facultad de Ciencias Universidad de Chile).
16. Hidalgo, P., and MacKinnon, R. (1995). Revealing the architecture of a K channel pore through mutant cycles with a peptide inhibitor. Science 268, 307-310.
17. Horovitz, A., and Fersht, A.R. (1990). Strategy for analysing the cooperativity of intramolecuar interactions in peptides and proteins. J. Mol. Biol. 214, 613-617.]
18. Hoshi, T., Zagotta, W.N., and Aldrich, R.W. (1990). Biophysical and molecular mechanisms of Shaker potassium channel inactivation. Science 250, 533-538.
19. Janin, J., and Chothia, C. (1990). The Structure of protein-protein recognition sites. J. Biol. Chem. 265, 16027-16030.
20. Johnson, B.A., and Sugg, E.E. (1992). Determination of the three-dimensional structure of iberiotoxin in solution by 1H nuclear magnetic resonance spectroscopy. Biochemistry 31, 8151-8159.
21. Kamb, A., Iverson, L.E., and Tanouye, M.A. (1987). Molecular characterization of Shaker, a Drosophila gene that encodes a potassium channel. Cell 50, 405-413.
22. Krezel, A.M., Kasibhatla, C., Hidalgo, P., MacKinnon, R., and Wagner, G. (1995). Solution structure of the potassium channel inhibitor agitoxin 2: caliper for probing channel geometry. Prot. Sci. 4, 1478-1489.
23. Lu, Z., and MacKinnon, R. (1994). A conductance maximum observed in an inward-rectifier potassium channel. J. Gen. Physiol. 104, 477-485.
24. MacKinnon, R. (1991). Determination of the subunit stoichiometry of a voltage-activated potassium channel. Nature 350, 232-235.
25. MacKinnon, R. (1995). Pore loops: an emerging theme in ion channel structure. Neuron 14, 889-892.
26. + channels. J. Gen. Physiol. 91, 335-349.
27. + channel-blocking peptides. Neuron 15, 5-10.
28. Nicholls, A., Sharp, K.A., and Honig, B. (1995). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Prot. Struct. Funct. Genet. 11, 281-296.
29. + channel. Neuron 9, 307-313.
30. + channels. Proc. Natl. Acad. Sci. USA 88, 2046-2050.
31. Schreiber, G., and Fersht, A.R. (1995). Energetics of protein-protein interactions: analysis of the Barnase-Barstar interface by single mutations and double mutant cycles. J. Mol. Biol. 248, 478-486.
32. + channel structure from a complete functional map of the molecular surface of charybdotoxin. Biochemistry 33, 443-450.
33. Stocker, M., and Miller, C. (1994). Electrostatic distance geometry in a K channel vestibule. Proc. Natl. Acad. Sci. USA 91, 9509-9513.
34. + channel. Science 251, 939-941.