{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T00:18:43Z","timestamp":1791332323227,"version":"4.3.1"},"reference-count":30,"publisher":"National Academy of Sciences","issue":"8","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2017,2,21]]},"abstract":"<jats:title>Significance<\/jats:title>\n                  <jats:p>\n                    The A\n                    <jats:sub>2A<\/jats:sub>\n                    R is a G protein-coupled receptor (GPCR) that plays important roles in cardiovascular physiology and immune function. The A\n                    <jats:sub>2A<\/jats:sub>\n                    R is also a target for the treatment of Parkinson\u2019s disease, where A\n                    <jats:sub>2A<\/jats:sub>\n                    R antagonists have been shown to enhance signaling through the D2 dopamine receptor. Here we present the crystal structure of the A\n                    <jats:sub>2A<\/jats:sub>\n                    R bound to a novel bitopic antagonist. As a result of structural changes needed to accommodate the bound antagonist, crystals could not be grown in lipidic cubic phase. Instead, crystals were grown in detergent with a type II packing rarely observed in GPCR crystals. The structure revealed a potential allosteric pocket that that can be exploited to develop subtype-selective allosteric modulators.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1621423114","type":"journal-article","created":{"date-parts":[[2017,2,6]],"date-time":"2017-02-06T21:05:30Z","timestamp":1486415130000},"page":"2066-2071","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":130,"title":["Crystal structure of the adenosine A\n                    <sub>2A<\/sub>\n                    receptor bound to an antagonist reveals a potential allosteric pocket"],"prefix":"10.1073","volume":"114","author":[{"given":"Bingfa","family":"Sun","sequence":"first","affiliation":[{"name":"ConfometRx, Inc., Santa Clara, CA 95054;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Priti","family":"Bachhawat","sequence":"additional","affiliation":[{"name":"ConfometRx, Inc., Santa Clara, CA 95054;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthew Ling-Hon","family":"Chu","sequence":"additional","affiliation":[{"name":"ConfometRx, Inc., Santa Clara, CA 95054;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martyn","family":"Wood","sequence":"additional","affiliation":[{"name":"Discovery Biology, New Medicines, UCB Pharma, B-1420 Braine-l\u2019Alleud, Belgium;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tom","family":"Ceska","sequence":"additional","affiliation":[{"name":"Department of Structural Biology, New Medicines, UCB Pharma, Slough SL1 3WE, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zara A.","family":"Sands","sequence":"additional","affiliation":[{"name":"Discovery Chemistry, New Medicines, UCB Pharma, B-1420 Braine-l\u2019Alleud, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joel","family":"Mercier","sequence":"additional","affiliation":[{"name":"Discovery Chemistry, New Medicines, UCB Pharma, B-1420 Braine-l\u2019Alleud, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Florence","family":"Lebon","sequence":"additional","affiliation":[{"name":"Discovery Chemistry, New Medicines, UCB Pharma, B-1420 Braine-l\u2019Alleud, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tong Sun","family":"Kobilka","sequence":"additional","affiliation":[{"name":"ConfometRx, Inc., Santa Clara, CA 95054;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brian K.","family":"Kobilka","sequence":"additional","affiliation":[{"name":"ConfometRx, Inc., Santa Clara, CA 95054;"},{"name":"Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2017,2,6]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"crossref","first-page":"3623","DOI":"10.1021\/jm4011669","article-title":"Adenosine A2A receptor as a drug discovery target","volume":"57","author":"de Lera Ruiz M","year":"2014","unstructured":"M de Lera Ruiz, YH Lim, J Zheng, Adenosine A2A receptor as a drug discovery target. 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