Structure of the carboxy-terminal region of a KCNH channel

Nature

Volumn 481, Issue 7382, 2012, Pages 530-533

  Brelidze, Tinatin I ^a   Carlson, Anne E ^a   Sankaran, Banumathi ^b   Zagotta, William N ^a  

^a UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

^b LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC NUCLEOTIDE; CYCLIC NUCLEOTIDE BINDING HOMOLOGY DOMAIN; DIMER; ION CHANNEL; POTASSIUM CHANNEL HERG; UNCLASSIFIED DRUG; VOLTAGE DEPENDENT ANION CHANNEL; VOLTAGE GATED POTASSIUM CHANNEL;

CARBOXYLIC ACID; CELL ORGANELLE; CYANIDE; DRUG; HOMOGENEITY; ION; POLARIZATION; POTASSIUM; RESOLUTION; TUMOR;

ANIMAL EXPERIMENT; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; ELECTROPHYSIOLOGY; HYPERPOLARIZATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN QUATERNARY STRUCTURE; STATIC ELECTRICITY; X RAY ANALYSIS; ZEBRA FISH;

ANIMALS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ELECTROPHYSIOLOGICAL PHENOMENA; ETHER-A-GO-GO POTASSIUM CHANNELS; ION CHANNELS; MODELS, MOLECULAR; MUTATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; STATIC ELECTRICITY; STRUCTURE-ACTIVITY RELATIONSHIP; ZEBRAFISH; ZEBRAFISH PROTEINS;

DANIO RERIO;

EID: 84856234056     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature10735     Document Type: Article

References (39)

1. Sanguinetti, M. C. & Tristani-Firouzi, M. hERG potassium channels and cardiac arrhythmia. Nature 440, 463-469 (2006).
2. Zhang, X. et al. Deletion of the potassium channel Kv12.2 causes hippocampal hyperexcitability and epilepsy. Nature Neurosci. 13, 1056-1058 (2010).
3. Camacho, J. Ether à go-go potassium channels and cancer. Cancer Lett. 233, 1-9 (2006).
4. Ganetzky, B., Robertson, G. A., Wilson, G. F., Trudeau, M. C. & Titus, S. A. The Eag family of K1 channels in Drosophila and mammals. Ann. NY Acad. Sci. 868, 356-369 (1999).
5. Al-Owais, M., Bracey, K. & Wray, D. Role of intracellular domains in the function of the herg potassium channel. Eur. Biophys. J. 38, 569-576 (2009).
6. Stevens, L., Ju, M. & Wray, D. Roles of surface residues of intracellular domains of heag potassium channels. Eur. Biophys. J. 38, 523-532 (2009).
7. Gustina, A. S. & Trudeau, M. C. hERG potassium channel gating is mediated by Nand C-terminal region interactions. J. Gen. Physiol. 137, 315-325 (2011).
8. Muskett, F. W. et al. Mechanistic insight into human ether-à-go- go-related gene (hERG) K1 channel deactivation gating from the solution structure of the EAG domain. J. Biol. Chem. 286, 6184-6191 (2011).
9. Zhou, Z., Gong, Q., Epstein, M. L. & January, C. T. HERG channel dysfunction in human long QT syndrome. Intracellular transport and functional defects. J. Biol. Chem. 273, 21061-21066 (1998).
10. Zagotta, W. N. et al. Structural basis for modulation and agonist specificity of HCN pacemaker channels. Nature 425, 200-205 (2003).
11. Brelidze, T. I., Carlson, A. E. & Zagotta, W. N. Absence of direct cyclic nucleotide modulation of mEAG1 and hERG1 channels revealed with fluorescence and electrophysiological methods. J. Biol. Chem. 284, 27989-27997 (2009).
12. Morais Cabral, J. H. et al. Crystal structure and functional analysis of the HERG potassium channel N terminus: a eukaryotic PAS domain. Cell 95, 649-655 (1998).
13. Schonherr, R. & Heinemann, S. H. Molecular determinants for activation and inactivation of HERG, a human inward rectifier potassium channel. J. Physiol. (Lond.) 493, 635-642 (1996).
14. Wang, J., Trudeau, M. C., Zappia, A. M.& Robertson, G. A. Regulation of deactivation by an amino terminal domain in human ether-à-go-go- related gene potassium channels. J. Gen. Physiol. 112, 637-647 (1998).
15. Muskett, F. W. et al. Mechanistic insight into hERG K1 channel deactivation gating from the solution structure of the EAG domain. J. Biol. Chem. 286, 6184-6191 (2011).
16. Li, Q. et al. NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker. Biochem. Biophys. Res. Commun. 403, 126-132 (2010).
17. Ng, C. A. et al. The N-terminal tail of hERG contains an amphipathic a-helix that regulates channel deactivation. PLoS ONE 6, e16191 (2011).
18. Craven, K. B. & Zagotta, W. N. CNG and HCN channels: two peas, one pod. Annu. Rev. Physiol. 68, 375-401 (2006).
19. Brelidze, T. I., Carlson, A. E., Davies, D. R., Stewart, L. J. & Zagotta, W. N. Identifying regulators for EAG1 channels with a novel electrophysiology and tryptophan fluorescence based screen. PLoS ONE 5, e12523 (2010).
20. Splawski, I. et al. Spectrum of mutations in long-QT syndrome genes. KVLQT1, HERG, SCN5A, KCNE1, and KCNE2. Circulation 102, 1178-1185 (2000).
21. Kawate, T. & Gouaux, E. Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins. Structure 14, 673-681 (2006).
22. Becchetti, A. et al. The functional properties of the human ether-à-go-go-like (HELK2) K1 channel. Eur. J. Neurosci. 16, 415-428 (2002).
23. Engeland, B., Neu, A., Ludwig, J., Roeper, J. & Pongs, O. Cloning and functional expression of rat ether-à-go-go-like K1 channel genes. J. Physiol. (Lond.) 513, 647-654 (1998).
24. Trudeau, M. C., Titus, S. A., Branchaw, J. L., Ganetzky, B. & Robertson, G. A. Functional analysis of a mouse brain Elk-type K1 channel. J. Neurosci. 19, 2906-2918 (1999).
25. Zou, A. et al. Distribution and functional properties of human KCNH8 (Elk1) potassium channels. Am. J. Physiol. Cell Physiol. 285, C1356-C1366 (2003).
26. Rehmann, H., Wittinghofer, A. & Bos, J. L. Capturing cyclic nucleotides in action: snapshots from crystallographic studies. Nature Rev. Mol. Cell Biol. 8, 63-73 (2007).
27. Altieri, S. L. et al. Structural and energetic analysis of activation by a cyclic nucleotide binding domain. J. Mol. Biol. 381, 655-669 (2008).
28. Clayton, G. M., Silverman, W. R., Heginbotham, L. & Morais-Cabral, J. H. Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel. Cell 119, 615-627 (2004).
29. Schunke, S., Stoldt, M., Lecher, J., Kaupp, U. B.&Willbold, D. Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel. Proc. Natl Acad. Sci. USA 108, 6121-6126 (2011).
30. Napolitano, C. et al. Genetic testing in the long QT syndrome: development and validation of an efficient approach to genotyping in clinical practice. J. Am. Med. Assoc. 294, 2975-2980 (2005).
31. Guerrero, S. A., Hecht, H. J., Hofmann, B., Biebl, H. & Singh, M. Production of selenomethionine-labelled proteins using simplified culture conditions and generally applicable host/vector systems. Appl. Microbiol. Biotechnol. 56, 718-723 (2001).
32. Collaborative Computation Project 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
33. Otwinowski, Z.& Minor, W. Processing X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
34. Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213-221 (2010).
35. Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
36. Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D 66, 12-21 (2010).
37. DeLano, W. L. The PyMOL molecular graphics system. http://www.pymol.org (DeLano Scientific, 2002).
38. Huson, D. H. et al. Dendroscope: an interactive viewer for large phylogenetic trees. BMC Bioinformatics 8, 460 (2007).
39. Baker, N. A., Sept, D., Joseph, S., Holst, M. J. & McCammon, J. A. Electrostatics of nanosystems: application to microtubules and the ribosome. Proc. Natl Acad. Sci. USA 98, 10037-10041 (2001).