K2P channel gating mechanisms revealed by structures of TREK-2 and a complex with Prozac

Science

Volumn 347, Issue 6227, 2015, Pages 1256-1259

  Dong, Yin Yao ^a   Pike, Ashley C W ^a   Mackenzie, Alexandra ^a,b   McClenaghan, Conor ^b   Aryal, Prafulla ^a,b   Dong, Liang ^a,e   Quigley, Andrew ^a   Grieben, Mariana ^a   Goubin, Solenne ^a,f   Mukhopadhyay, Shubhashish ^a   Ruda, Gian Filippo ^a,c   Clausen, Michael V ^b   Cao, Lishuang ^d   Brennan, Paul E ^a,c   Burgess Brown, Nicola A ^a   Sansom, Mark S P ^a,b   Tucker, Stephen J ^b   Carpenter, Elisabeth P ^a,b  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c UNIVERSITY OF OXFORD   (United Kingdom)

^d PFIZER GLOBAL RESEARCH AND DEVELOPMENT   (United Kingdom)

^e UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^f UNIVERSITY OF NOTTINGHAM   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ARACHIDONIC ACID; FLUOXETINE; NORFLUOXETINE; POTASSIUM CHANNEL; POTASSIUM CHANNEL TREK 2; UNCLASSIFIED DRUG; KCNK10 PROTEIN, HUMAN; POTASSIUM; TANDEM PORE DOMAIN POTASSIUM CHANNEL;

ANTIDEPRESSANT ACTIVITY; ARTICLE; CHANNEL GATING; CRYSTAL STRUCTURE; DEPRESSION; DRUG BINDING SITE; DRUG CONFORMATION; DRUG MECHANISM; DRUG PROTEIN BINDING; HUMAN; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MUTATION; NONHUMAN; PRIORITY JOURNAL; WILD TYPE; AMINO ACID SEQUENCE; ANALOGS AND DERIVATIVES; ANTAGONISTS AND INHIBITORS; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ARACHIDONIC ACID; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; FLUOXETINE; HUMANS; ION CHANNEL GATING; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; MOLECULAR SEQUENCE DATA; POTASSIUM; POTASSIUM CHANNELS, TANDEM PORE DOMAIN; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 84924778497     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1261512     Document Type: Article

References (30)

1. P. Enyedi, G. Czirják, Physiol. Rev. 90, 559-605 (2010).
2. A. Cohen, Y. Ben-Abu, N. Zilberberg, Eur. Biophys. J. 39, 61-73 (2009).
3. J. Noël, G. Sandoz, F. Lesage, Channels 5, 402-409 (2011).
4. L. E. Kennard et al., Br. J. Pharmacol. 144, 821-829 (2005).
5. C. Heurteaux et al., Nat. Neurosci. 9, 1134-1141 (2006).
6. Z. Es-Salah-Lamoureux, D. F. Steele, D. Fedida, Trends Pharmacol. Sci. 31, 587-595 (2010).
7. M. E. Henry et al., Neuropsychopharmacology 30, 1576-1583 (2005).
8. E. Honoré, Nat. Rev. Neurosci. 8, 251-261 (2007).
9. A. Gurney, B. Manoury, Eur. Biophys. J. 38, 305-318 (2009).
10. S. G. Brohawn, E. B. Campbell, R. MacKinnon, Proc. Natl. Acad. Sci. U.S.A. 110, 2129-2134 (2013).
11. S. G. Brohawn, J. del Mármol, R. MacKinnon, Science 335, 436-441 (2012).
12. A. N. Miller, S. B. Long, Science 335, 432-436 (2012).
13. S. N. Bagriantsev, R. Peyronnet, K. A. Clark, E. Honoré, D. L. Minor Jr., EMBO J. 30, 3594-3606 (2011).
14. P. L. Piechotta et al., EMBO J. 30, 3607-3619 (2011).
15. Materials and methods are available as supplementary materials on Science Online.
16. S. G. Brohawn, E. B. Campbell, R. MacKinnon, Nature 516, 126-130 (2014).
17. M. Lolicato, P. M. Riegelhaupt, C. Arrigoni, K. A. Clark, D. L. Minor Jr., Neuron 84, 1198-1212 (2014).
18. M. Zhou, J. H. Morais-Cabral, S. Mann, R. MacKinnon, Nature 411, 657-661 (2001).
19. D. A. Köpfer et al., Science 346, 352-355 (2014).
20. Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
21. E. Honoré, F. Maingret, M. Lazdunski, A. J. Patel, EMBO J. 21, 2968-2976 (2002).
22. F. Maingret, A. J. Patel, F. Lesage, M. Lazdunski, E. Honoré, J. Biol. Chem. 274, 26691-26696 (1999).
23. S. N. Bagriantsev, K. A. Clark, D. L. Minor Jr., EMBO J. 31, 3297-3308 (2012).
24. J. Chemin et al., Pflugers Arch. 455, 97-103 (2007).
25. G. Sandoz, D. Douguet, F. Chatelain, M. Lazdunski, F. Lesage, Proc. Natl. Acad. Sci. U.S.A. 106, 14628-14633 (2009).
26. A. Anishkin, S. H. Loukin, J. Teng, C. Kung, Proc. Natl. Acad. Sci. U.S.A. 111, 7898-7905 (2014).
27. S. G. Brohawn, Z. Su, R. MacKinnon, Proc. Natl. Acad. Sci. U.S.A. 111, 3614-3619 (2014).
28. J. Teng, S. Loukin, A. Anishkin, C. Kung, Pflugers Arch. 467, 27-37 (2015).
29. P. Aryal, F. Abd-Wahab, G. Bucci, M. S. Sansom, S. J. Tucker, Nat. Commun. 5, 4377 (2014).
30. P. Aryal, F. Abd-Wahab, G. Bucci, M. S. Sansom, S. J. Tucker, Channels 9, 44-49 (2015).