Structural Features for Functional Selectivity at Serotonin Receptors
Drugs active at G protein–coupled receptors (GPCRs) can differentially modulate either canonical or noncanonical signaling pathways via a phenomenon known as functional selectivity or biased signaling. We report biochemical studies showing that the hallucinogen lysergic acid diethylamide, its precur...
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| Veröffentlicht in: | Science 2013-05, Vol.340 (6132), p.615-619 |
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| creator | Wacker, Daniel Wang, Chong Katritch, Vsevolod Han, Gye Won Huang, Xi-Ping Vardy, Eyal McCorvy, John D. Jiang, Yi Chu, Meihua Siu, Fai Yiu Liu, Wei Xu, H. Eric Cherezov, Vadim Roth, Bryan L. Stevens, Raymond C. |
| description | Drugs active at G protein–coupled receptors (GPCRs) can differentially modulate either canonical or noncanonical signaling pathways via a phenomenon known as functional selectivity or biased signaling. We report biochemical studies showing that the hallucinogen lysergic acid diethylamide, its precursor ergotamine (ERG), and related ergolines display strong functional selectivity for β-arrestin signaling at the 5-HT 2B 5-hydroxytryptamine (5-HT) receptor, whereas they are relatively unbiased at the 5-HT 1B receptor. To investigate the structural basis for biased signaling, we determined the crystal structure of the human 5-HT 2B receptor bound to ERG and compared it with the 5-HT 1B /ERG structure. Given the relatively poor understanding of GPCR structure and function to date, insight into different GPCR signaling pathways is important to better understand both adverse and favorable therapeutic activities. |
| doi_str_mv | 10.1126/science.1232808 |
| format | Article |
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Eric ; Cherezov, Vadim ; Roth, Bryan L. ; Stevens, Raymond C.</creator><creatorcontrib>Wacker, Daniel ; Wang, Chong ; Katritch, Vsevolod ; Han, Gye Won ; Huang, Xi-Ping ; Vardy, Eyal ; McCorvy, John D. ; Jiang, Yi ; Chu, Meihua ; Siu, Fai Yiu ; Liu, Wei ; Xu, H. Eric ; Cherezov, Vadim ; Roth, Bryan L. ; Stevens, Raymond C. ; Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><description>Drugs active at G protein–coupled receptors (GPCRs) can differentially modulate either canonical or noncanonical signaling pathways via a phenomenon known as functional selectivity or biased signaling. We report biochemical studies showing that the hallucinogen lysergic acid diethylamide, its precursor ergotamine (ERG), and related ergolines display strong functional selectivity for β-arrestin signaling at the 5-HT 2B 5-hydroxytryptamine (5-HT) receptor, whereas they are relatively unbiased at the 5-HT 1B receptor. To investigate the structural basis for biased signaling, we determined the crystal structure of the human 5-HT 2B receptor bound to ERG and compared it with the 5-HT 1B /ERG structure. Given the relatively poor understanding of GPCR structure and function to date, insight into different GPCR signaling pathways is important to better understand both adverse and favorable therapeutic activities.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1232808</identifier><identifier>PMID: 23519215</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>United States: American Association for the Advancement of Science</publisher><subject>Agonists ; Amino Acid Motifs ; Amino Acid Sequence ; Arrestin - metabolism ; Arrestins - metabolism ; beta-Arrestins ; Binding Sites ; Biochemistry ; Crystal structure ; Crystallography, X-Ray ; drugs ; Ergolines - chemistry ; Ergolines - metabolism ; Ergotamine - chemistry ; Ergotamine - metabolism ; Grants ; headache ; HEK293 Cells ; Humans ; Hydrogen bonds ; Ligands ; Lysergic Acid Diethylamide ; Lysergic Acid Diethylamide - chemistry ; Lysergic Acid Diethylamide - metabolism ; migraine ; Models, Molecular ; Molecular Sequence Data ; Narcotics ; Neurons ; Obesity ; Pharmacology ; Protein Conformation ; Protein Structure, Secondary ; Receptor, Serotonin, 5-HT1B - chemistry ; Receptor, Serotonin, 5-HT1B - metabolism ; Receptor, Serotonin, 5-HT2B - chemistry ; Receptor, Serotonin, 5-HT2B - metabolism ; Receptors ; Receptors, Serotonin - chemistry ; Receptors, Serotonin - metabolism ; Sand sheets ; Serotonin ; Serotonin receptors ; Signal Transduction</subject><ispartof>Science, 2013-05, Vol.340 (6132), p.615-619</ispartof><rights>Copyright © 2013 American Association for the Advancement of Science</rights><rights>Copyright © 2013, American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c569t-99622726f5de5d87bfc33a4f915209f9af5fa1230e7c10936f5f4d1b3486cbaa3</citedby><cites>FETCH-LOGICAL-c569t-99622726f5de5d87bfc33a4f915209f9af5fa1230e7c10936f5f4d1b3486cbaa3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/41985012$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/41985012$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,776,780,799,881,2871,2872,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23519215$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1081344$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Wacker, Daniel</creatorcontrib><creatorcontrib>Wang, Chong</creatorcontrib><creatorcontrib>Katritch, Vsevolod</creatorcontrib><creatorcontrib>Han, Gye Won</creatorcontrib><creatorcontrib>Huang, Xi-Ping</creatorcontrib><creatorcontrib>Vardy, Eyal</creatorcontrib><creatorcontrib>McCorvy, John D.</creatorcontrib><creatorcontrib>Jiang, Yi</creatorcontrib><creatorcontrib>Chu, Meihua</creatorcontrib><creatorcontrib>Siu, Fai Yiu</creatorcontrib><creatorcontrib>Liu, Wei</creatorcontrib><creatorcontrib>Xu, H. Eric</creatorcontrib><creatorcontrib>Cherezov, Vadim</creatorcontrib><creatorcontrib>Roth, Bryan L.</creatorcontrib><creatorcontrib>Stevens, Raymond C.</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><title>Structural Features for Functional Selectivity at Serotonin Receptors</title><title>Science</title><addtitle>Science</addtitle><description>Drugs active at G protein–coupled receptors (GPCRs) can differentially modulate either canonical or noncanonical signaling pathways via a phenomenon known as functional selectivity or biased signaling. We report biochemical studies showing that the hallucinogen lysergic acid diethylamide, its precursor ergotamine (ERG), and related ergolines display strong functional selectivity for β-arrestin signaling at the 5-HT 2B 5-hydroxytryptamine (5-HT) receptor, whereas they are relatively unbiased at the 5-HT 1B receptor. To investigate the structural basis for biased signaling, we determined the crystal structure of the human 5-HT 2B receptor bound to ERG and compared it with the 5-HT 1B /ERG structure. Given the relatively poor understanding of GPCR structure and function to date, insight into different GPCR signaling pathways is important to better understand both adverse and favorable therapeutic activities.</description><subject>Agonists</subject><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Arrestin - metabolism</subject><subject>Arrestins - metabolism</subject><subject>beta-Arrestins</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>drugs</subject><subject>Ergolines - chemistry</subject><subject>Ergolines - metabolism</subject><subject>Ergotamine - chemistry</subject><subject>Ergotamine - metabolism</subject><subject>Grants</subject><subject>headache</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Hydrogen bonds</subject><subject>Ligands</subject><subject>Lysergic Acid Diethylamide</subject><subject>Lysergic Acid Diethylamide - chemistry</subject><subject>Lysergic Acid Diethylamide - metabolism</subject><subject>migraine</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Narcotics</subject><subject>Neurons</subject><subject>Obesity</subject><subject>Pharmacology</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><subject>Receptor, Serotonin, 5-HT1B - chemistry</subject><subject>Receptor, Serotonin, 5-HT1B - metabolism</subject><subject>Receptor, Serotonin, 5-HT2B - chemistry</subject><subject>Receptor, Serotonin, 5-HT2B - metabolism</subject><subject>Receptors</subject><subject>Receptors, Serotonin - chemistry</subject><subject>Receptors, Serotonin - metabolism</subject><subject>Sand sheets</subject><subject>Serotonin</subject><subject>Serotonin receptors</subject><subject>Signal Transduction</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1PGzEQhi1UBGnouSfQqr30suCP9e76UqlCpCAhIUF7thxnXBxt7NT2IvHvO2jTqOXCyWPP43c-XkI-MnrOGG8vsvUQLJwzLnhP-wMyY1TJWnEq3pEZpaKte9rJY_I-5zWlmFPiiBxzIZniTM7I1UNJoy1jMkO1AIMB5MrFVC3GYIuPAd8fYACMn3x5rkzBa4olBh-qe7CwLTHlE3LozJDhw-6ck5-Lqx-X1_Xt3feby2-3tZWtKrVSLecdb51cgVz13dJZIUzjFJOcKqeMk87gKBQ6i3MIBF2zYkvR9K1dGiPm5Oukux2XG1hZCAUb19vkNyY962i8_j8T_KP-FZ-0aJtGKIoCnyaBmIvXuL0C9tHGEHBAzWjPBHJz8mVXJcXfI-SiNz5bGAYTII5Zc1yk6Bjl_E0U9XpJm0a-lP78Cl3HMeF-J4oq1rMOqYuJsinmnMDth2NUv1iud5brneX44-zfnez5vx4jcDoB64xe7fMNU9gaqvwB4Bmx3A</recordid><startdate>20130503</startdate><enddate>20130503</enddate><creator>Wacker, Daniel</creator><creator>Wang, Chong</creator><creator>Katritch, Vsevolod</creator><creator>Han, Gye Won</creator><creator>Huang, Xi-Ping</creator><creator>Vardy, Eyal</creator><creator>McCorvy, John D.</creator><creator>Jiang, Yi</creator><creator>Chu, Meihua</creator><creator>Siu, Fai Yiu</creator><creator>Liu, Wei</creator><creator>Xu, H. 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Eric</creatorcontrib><creatorcontrib>Cherezov, Vadim</creatorcontrib><creatorcontrib>Roth, Bryan L.</creatorcontrib><creatorcontrib>Stevens, Raymond C.</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). 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Eric</au><au>Cherezov, Vadim</au><au>Roth, Bryan L.</au><au>Stevens, Raymond C.</au><aucorp>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural Features for Functional Selectivity at Serotonin Receptors</atitle><jtitle>Science</jtitle><addtitle>Science</addtitle><date>2013-05-03</date><risdate>2013</risdate><volume>340</volume><issue>6132</issue><spage>615</spage><epage>619</epage><pages>615-619</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>Drugs active at G protein–coupled receptors (GPCRs) can differentially modulate either canonical or noncanonical signaling pathways via a phenomenon known as functional selectivity or biased signaling. We report biochemical studies showing that the hallucinogen lysergic acid diethylamide, its precursor ergotamine (ERG), and related ergolines display strong functional selectivity for β-arrestin signaling at the 5-HT 2B 5-hydroxytryptamine (5-HT) receptor, whereas they are relatively unbiased at the 5-HT 1B receptor. To investigate the structural basis for biased signaling, we determined the crystal structure of the human 5-HT 2B receptor bound to ERG and compared it with the 5-HT 1B /ERG structure. Given the relatively poor understanding of GPCR structure and function to date, insight into different GPCR signaling pathways is important to better understand both adverse and favorable therapeutic activities.</abstract><cop>United States</cop><pub>American Association for the Advancement of Science</pub><pmid>23519215</pmid><doi>10.1126/science.1232808</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Science, 2013-05, Vol.340 (6132), p.615-619 |
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| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| subjects | Agonists Amino Acid Motifs Amino Acid Sequence Arrestin - metabolism Arrestins - metabolism beta-Arrestins Binding Sites Biochemistry Crystal structure Crystallography, X-Ray drugs Ergolines - chemistry Ergolines - metabolism Ergotamine - chemistry Ergotamine - metabolism Grants headache HEK293 Cells Humans Hydrogen bonds Ligands Lysergic Acid Diethylamide Lysergic Acid Diethylamide - chemistry Lysergic Acid Diethylamide - metabolism migraine Models, Molecular Molecular Sequence Data Narcotics Neurons Obesity Pharmacology Protein Conformation Protein Structure, Secondary Receptor, Serotonin, 5-HT1B - chemistry Receptor, Serotonin, 5-HT1B - metabolism Receptor, Serotonin, 5-HT2B - chemistry Receptor, Serotonin, 5-HT2B - metabolism Receptors Receptors, Serotonin - chemistry Receptors, Serotonin - metabolism Sand sheets Serotonin Serotonin receptors Signal Transduction |
| title | Structural Features for Functional Selectivity at Serotonin Receptors |
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