D4 dopamine receptor high-resolution structures enable the discovery of selective agonists

Science

Volumn 358, Issue 6361, 2017, Pages 381-386

  Wang, Sheng ^a   Wacker, Daniel ^a   Levit, Anat ^b   Che, Tao ^a   Betz, Robin M ^c,d,e   McCorvy, John D ^a   Venkatakrishnan, A J ^c,d   Huang, Xi Ping ^a   Dror, Ron O ^c,d,e   Shoichet, Brian K ^b   Roth, Bryan L ^a,f  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c Stanford University   (United States)

^d STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^e STANFORD UNIVERSITY   (United States)

^f University of North Carolina   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DOPAMINE 4 RECEPTOR; DOPAMINE RECEPTOR AFFECTING AGENT; EMONAPRIDE; QUINPIROLE; BENZAMIDE DERIVATIVE; DOPAMINE RECEPTOR STIMULATING AGENT; DRD4 PROTEIN, HUMAN; NEUROLEPTIC AGENT;

CRYSTAL STRUCTURE; DRUG; GENETIC ANALYSIS; MOLECULAR ANALYSIS; NERVOUS SYSTEM DISORDER; NEUROLOGY; PATHOGENICITY; RESOLUTION;

ALLOSTERISM; ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DRUG STRUCTURE; GENE MUTATION; HUMAN; HYDROGEN BOND; INHIBITION CONSTANT; LIGAND BINDING; PRIORITY JOURNAL; ALLOSTERIC SITE; CHEMISTRY; ISOLATION AND PURIFICATION; PROTEIN CONFORMATION; STRUCTURE ACTIVITY RELATION; ULTRASTRUCTURE;

ALLOSTERIC SITE; ANTIPSYCHOTIC AGENTS; BENZAMIDES; DOPAMINE AGONISTS; HUMANS; PROTEIN CONFORMATION; RECEPTORS, DOPAMINE D4; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 85032508115     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aan5468     Document Type: Article

References (25)

1. C. Missale, S. R. Nash, S. W. Robinson, M. Jaber, M. G. Caron, Physiol. Rev. 78, 189-225 (1998).
2. J. M. Beaulieu, S. Espinoza, R. R. Gainetdinov, Br. J. Pharmacol. 172, 1-23 (2015).
3. E. Y. Chien et al., Science 330, 1091-1095 (2010).
4. R. Chu et al., J. Mol. Biol. 323, 253-262 (2002).
5. S. G. Rasmussen et al., Nature 477, 549-555 (2011).
6. W. Liu et al., Science 337, 232-236 (2012).
7. G. Fenalti et al., Nature 506, 191-196 (2014).
8. J. L. Miller-Gallacher et al., PLOS ONE 9, e92727 (2014).
9. C. Zhang et al., Nature 492, 387-392 (2012).
10. V. Katritch et al., Trends Biochem. Sci. 39, 233-244 (2014).
11. H. Gutiérrez-de-Terán et al., Structure 21, 2175-2185 (2013).
12. O. N. Vickery, J. P. Machtens, G. Tamburrino, D. Seeliger, U. Zachariae, Structure 24, 997-1007 (2016).
13. K. A. Neve, Mol. Pharmacol. 39, 570-578 (1991).
14. M. Michino, R. B. Free, T. B. Doyle, D. R. Sibley, L. Shi, Chem. Commun. (Camb.) 51, 8618-8621 (2015).
15. M. M. Simpson et al., Mol. Pharmacol. 56, 1116-1126 (1999).
16. J. A. Schetz, P. S. Benjamin, D. R. Sibley, Mol. Pharmacol. 57, 144-152 (2000).
17. A. H. Newman et al., J. Med. Chem. 55, 6689-6699 (2012).
18. M. Michino et al., Mol. Pharmacol. 84, 854-864 (2013).
19. T. I. Oprea, A. M. Davis, S. J. Teague, P. D. Leeson, J. Chem. Inf. Comput. Sci. 41, 1308-1315 (2001).
20. T. Sterling, J. J. Irwin, J. Chem. Inf. Model. 55, 2324-2337 (2015).
21. A. Manglik et al., Nature 537, 185-190 (2016).
22. K. Lansu et al., Nat. Chem. Biol. 13, 529-536 (2017).
23. A. P. Bento et al., Nucleic Acids Res. 42, D1083-D1090 (2014).
24. A. Negri et al., J. Chem. Inf. Model. 53, 521-526 (2013).
25. D. Wacker et al., Cell 168, 377-389.e12 (2017).