NMR-derived dynamic aspects of N-type inactivation of a Kv channel suggest a transient interaction with the T1 domain

Biochemistry

Volumn 45, Issue 6, 2006, Pages 1663-1672

  Baker, Kent A ^a   Hilty, Christian ^b,e   Peti, Wolfgang ^c,f   Prince, Alison ^d   Pfaffinger, Paul J ^d   Wider, Gerhard ^b   Wiithrich, Kurt ^b,c   Choe, Senyon ^a  

^a SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

^b ETH ZURICH   (Switzerland)

^c SCRIPPS RESEARCH INSTITUTE   (United States)

^d BAYLOR COLLEGE OF MEDICINE   (United States)

^e LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

^f BROWN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; AMINO ACIDS; CRYSTALLOGRAPHY; ELECTROPHYSIOLOGY; REACTION KINETICS;

N-TERMINAL INACTIVATION PEPTIDE; N-TYPE INACTIVATION; PREINACTIVATION SITE MODEL; TETRAMERIZATION;

NUCLEAR MAGNETIC RESONANCE;

CALCIUM CHANNEL N TYPE; VOLTAGE GATED POTASSIUM CHANNEL;

ACTION POTENTIAL; ALPHA CHAIN; APLYSIA; ARTICLE; CRYSTALLOGRAPHY; DERIVATIZATION; ELECTROPHYSIOLOGY; MEMBRANE DEPOLARIZATION; MOLECULAR INTERACTION; NUCLEAR MAGNETIC RESONANCE; POTASSIUM TRANSPORT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN LOCALIZATION;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; EUKARYOTIC CELLS; HUMANS; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SHAKER SUPERFAMILY OF POTASSIUM CHANNELS;

APLYSIA; EUKARYOTA;

EID: 32344440232     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0516430     Document Type: Article

References (39)

1. + channel gating kinetics by deletions in the S3-S4 linker, Proc. Natl. Acad. Sci. U.S.A. 98, 9617-9623.
2. Hille, B. (2001) Ion Channels of Excitable Membranes, 3rd ed., Sinauer Associates, Sunderland, MA.
3. Zhou, M., Morais-Cabral, J., Mann, S., and MacKinnon, R. (2001) Potassium channel receptor site for the inactivation gate and quarternary amine inhibitors, Nature 411, 657-661.
4. Yellen, G. (2002) The voltage-gated potassium channels and their relatives, Nature 419, 35-42.
5. Gu, C., Jan, Y. N., and Jan, L. Y. (2003) A conserved domain in axonal targeting of Kvl (Shaker) voltage-gated potassium channels, Science 301, 646-649.
6. Miller, C. (2003) A charged view of voltage-gated ion channels, Nat. Struct. Biol. 10, 422-424.
7. Roosild, T. P., Le, K. T., and Choe, S. (2004) Cytoplasmic gatekeepers of potassium channel flux: A structural perspective, Trends Biochem. Sci. 29, 39-45.
8. Hoshi, T., Zagotta, W. N., and Aldrich, R. W. (1990) Biophysical and molecular mechanisms of Shaker potassium channel inactivation, Science 250, 533-538.
9. Zagotta, W. N., Hoshi, T., and Aldrich, R. W, (1990) Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB, Science 250, 568-571.
10. Bezanilla, F., and Armstrong C. M. (1972) Negative conductance caused by entry of sodium and cesium ions into the potassium channels of squid axons, J. Gen. Physiol. 60, 588-608.
11. MacKinnon, R., Aldrich, R., and Lee, A. W. (1993) Functional stoichiometry of Shaker potassium channel inactivation, Science 262, 757-759.
12. Kreusch, A., Pfaffinger, P., Stevens, C. F., and Choe, S. (1998) Crystal structure of the tetramerization domain of the Shaker potassium channel, Nature 392, 945-948.
13. 2+-mediated and molecular determinants of tetramerization in Kv channels, Nat. Struct. Biol. 6, 38-43.
14. Sokolova, O., Kolmakova-Partensky, L., and Grigorieff, N. (2001) Three-dimensional structure of a voltage-gated potassium channel at 2.5 nm resolution, Structure 9, 215-220.
15. Cushman, S. J., Nanao, M. H., Kunjilwaar, K., Jahng, A. W., DeRubeis, D., Choe, S., and Pfaffinger, P. J. (2000) Voltage-dependent activation of potassium channels is coupled to T1 domain structure, Nat. Struct. Biol. 7, 403-407.
16. Choe, S., Kreusch, A., and Pfaffinger, P. J. (1999) Towards the three-dimensional structure of voltage-gated potassium channels, Trends Biochem. Sci. 24, 345-349.
17. + channel, Biochemistry 39, 10347-10352.
18. + channels, Science 289, 123-127.
19. Long, S. B., Campbell, E. B., and Mackinnon, R. (2005) Voltage sensor of Kv1.2: Structural basis of electromechanical coupling, Science 309, 897-903.
20. Antz, C., Geyer, M., Fakler, B., Schott, M. K., Guy, H. R., Frank, R., Ruppersberg, J. P., and Kalbitzer, H. R. (1997) NMR structure of inactivation gates from mammalian voltage-dependent potassium channels, Nature 385, 272-274.
21. + channel analyzed by NMR spectroscopy, Eur. Biophys. J. 27, 99-104.
22. Pervushin, K., Riek, R., Wider, G., and Wüthrich, K. (1997) Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution, Proc. Natl. Acad. Sci. U.S.A. 94, 12366-12371.
23. Marley, J., Lu, M., and Bracken, C. (2001) A method for efficient isotopic labeling of recombinant proteins, J. Biomol. NMR 20, 71-75.
24. LeMaster, D. M., and Richards, F. M. (1988) NMR sequential assignment of Escherichia coli thioredoxin utilizing random fractional deuteriation, Biochemistry 27, 142-150.
25. 15N heteronuclear NMR studies of Escherichia coli thioredoxin in samples isotopically labeled by residue type, Biochemistry 24, 7263-7268.
26. Salzmann, M., Pervushin, K., Wider, G., Senn, H., and Wüthrich, K. (1998) TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins, Proc. Natl. Acad. Sci. U.S.A. 95, 13585-13590.
27. 1H]-TROSY-HNCA for sequential assignments of large proteins, J. Biomol. NMR 14, 85-88.
28. Salzmann, M., Wider, G., Pervushin, K., Senn, H., and Wüthrich, K. (1999) TROSY-type triple-resonance experiments for sequential NMR assignments of large proteins, J. Am. Chem. Soc. 121, 844-848.
29. Grzesiek, S., Anglister, J., Hao, R., and Bax, A. (1993) Carbon-13 line narrowing by deuterium decoupling in deuterium/carbon-13/nitrogen-15 enriched proteins. Application to triple resonance 4D connectivity of sequential amides, J. Am. Chem. Soc. 115, 4369-4379.
30. 1M correlations in large proteins, J. Biomol. NMR 17, 195-202.
31. Zhu, G., Xia, Y. L., Nicholson, L. K., and Sze, K. H. (2000) Protein dynamics measurements by TROSY-based NMR experiments, J. Magn. Reson. 143, 423-426.
32. 1H]-TROSY, J. Biomol. NMR 12, 345-348.
33. Güntert, P., Dötsch, V., Wider, G., and Wüthrich, K. (1992) Processing of multidimensional NMR data with the new software PROSA, J. Biomol NMR 2, 619-629.
34. Bartels, C., Xia, T. H., Billeter, M., Güntert, P., and Wüthrich, K. (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, J. Biomol. NMR 6, 1-10.
35. Markley, J. L., Bax, A., Arata, Y., Hilbers, C. W., Kaptein, R., Sykes, B. D., Wright, P. E., and Wüthrich, K. (1998) Recommendations for the presentation of NMR structures of proteins and nucleic acids. IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy, J. Biomol. NMR 12, 1-23.
36. Battiste, J. L., and Wagner, G. (2000) Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data, Biochemistry 39, 5355-5365.
37. Kosen, P. A. (1989) Spin labeling of proteins, Methods Enzymol. 177, 86-121.
38. + channel, Nature 353, 86-90.
39. + channel, Nature 423, 33-41.