Structure of a nanobody-stabilized active state of the beta(2) adrenoceptor
DC Field | Value | Language |
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dc.contributor.author | Rasmussen, Soren G. F. | - |
dc.contributor.author | Choi, Hee-Jung | - |
dc.contributor.author | Fung, Juan Jose | - |
dc.contributor.author | Pardon, Els | - |
dc.contributor.author | Casarosa, Paola | - |
dc.contributor.author | Chae, Pil Seok | - |
dc.contributor.author | DeVree, Brian T. | - |
dc.contributor.author | Rosenbaum, Daniel M. | - |
dc.contributor.author | Thian, Foon Sun | - |
dc.contributor.author | Kobilka, Tong Sun | - |
dc.contributor.author | Schnapp, Andreas | - |
dc.contributor.author | Konetzki, Ingo | - |
dc.contributor.author | Sunahara, Roger K. | - |
dc.contributor.author | Gellman, Samuel H. | - |
dc.contributor.author | Pautsch, Alexander | - |
dc.contributor.author | Steyaert, Jan | - |
dc.contributor.author | Weis, William I. | - |
dc.contributor.author | Kobilka, Brian K. | - |
dc.date.accessioned | 2021-06-23T11:06:39Z | - |
dc.date.available | 2021-06-23T11:06:39Z | - |
dc.date.created | 2021-01-21 | - |
dc.date.issued | 2011-01 | - |
dc.identifier.issn | 0028-0836 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/38304 | - |
dc.description.abstract | G protein coupled receptors (GPCRs) exhibit a spectrum of functional behaviours in response to natural and synthetic ligands. Recent crystal structures provide insights into inactive states of several GPCRs. Efforts to obtain an agonist-bound active-state GPCR structure have proven difficult due to the inherent instability of this state in the absence of a G protein. We generated a camelid antibody fragment (nanobody) to the human beta(2) adrenergic receptor (beta(2)AR) that exhibits G protein-like behaviour, and obtained an agonist-bound, active-state crystal structure of the receptor-nanobody complex. Comparison with the inactive beta(2)AR structure reveals subtle changes in the binding pocket; however, these small changes are associated with an 11 angstrom outward movement of the cytoplasmic end of transmembrane segment 6, and rearrangements of transmembrane segments 5 and 7 that are remarkably similar to those observed in opsin, an active form of rhodopsin. This structure provides insights into the process of agonist binding and activation. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | Nature Publishing Group | - |
dc.title | Structure of a nanobody-stabilized active state of the beta(2) adrenoceptor | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Chae, Pil Seok | - |
dc.identifier.doi | 10.1038/nature09648 | - |
dc.identifier.scopusid | 2-s2.0-78651411166 | - |
dc.identifier.wosid | 000286143400030 | - |
dc.identifier.bibliographicCitation | Nature, v.469, no.7329, pp.175 - 180 | - |
dc.relation.isPartOf | Nature | - |
dc.citation.title | Nature | - |
dc.citation.volume | 469 | - |
dc.citation.number | 7329 | - |
dc.citation.startPage | 175 | - |
dc.citation.endPage | 180 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | LIGAND-BINDING | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | RHODOPSIN | - |
dc.subject.keywordPlus | CONFORMATIONS | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.identifier.url | https://www.nature.com/articles/nature09648 | - |
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