Unlocking the secrets of the gatekeeper: Methods for stabilizing and crystallizing GPCRs
DC Field | Value | Language |
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dc.contributor.author | Bertheleme, Nicolas | - |
dc.contributor.author | Chae, Pil Seok | - |
dc.contributor.author | Singh, Shweta | - |
dc.contributor.author | Mossakowska, Danuta | - |
dc.contributor.author | Hann, Michael M. | - |
dc.contributor.author | Smith, Kathrine J. | - |
dc.contributor.author | Hubbard, Julia A. | - |
dc.contributor.author | Dowell, Simon J. | - |
dc.contributor.author | Byrne, Bernadette | - |
dc.date.accessioned | 2021-06-23T02:05:45Z | - |
dc.date.available | 2021-06-23T02:05:45Z | - |
dc.date.created | 2021-01-21 | - |
dc.date.issued | 2013-11 | - |
dc.identifier.issn | 0005-2736 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/26368 | - |
dc.description.abstract | G-protein coupled receptors (GPCRs) are integral membrane cell surface receptors with key roles in mediating the cellular responses to a wide range of biologically relevant molecules including hormones, neurotransmitters and importantly the majority of currently available drugs. The first high-resolution, X-ray crystallographic structure of a GPCR, that of rhodopsin, was obtained in 2000. It took a further seven years for the next structure, that of the 32 adrenergic receptor. Remarkably, at the time of writing, there have been an astonishing 18 further independent high-resolution GPCR structures published in the last five years (overall total of 68 structures in different conformations or bound to different ligands). Of particular note is the recent structure of the 02 adrenergic receptor in complex with its cognate heterotrimeric G-protein revealing for the first time molecular details of the interaction between a GPCR and the complete G-protein. Together these structures have provided unprecedented detail into the mechanism of action of these incredibly important proteins. This review describes several key methodological advances that have made such extraordinarily fast progress possible. (C) 2013 Elsevier B.V. All rights reserved. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | Elsevier BV | - |
dc.title | Unlocking the secrets of the gatekeeper: Methods for stabilizing and crystallizing GPCRs | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Chae, Pil Seok | - |
dc.identifier.doi | 10.1016/j.bbamem.2013.07.013 | - |
dc.identifier.scopusid | 2-s2.0-84880983378 | - |
dc.identifier.wosid | 000326143200026 | - |
dc.identifier.bibliographicCitation | Biochimica et Biophysica Acta - Biomembranes, v.1828, no.11, pp.2583 - 2591 | - |
dc.relation.isPartOf | Biochimica et Biophysica Acta - Biomembranes | - |
dc.citation.title | Biochimica et Biophysica Acta - Biomembranes | - |
dc.citation.volume | 1828 | - |
dc.citation.number | 11 | - |
dc.citation.startPage | 2583 | - |
dc.citation.endPage | 2591 | - |
dc.type.rims | ART | - |
dc.type.docType | Review | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.subject.keywordPlus | ADENOSINE A(2A) RECEPTOR | - |
dc.subject.keywordPlus | SENSORY RHODOPSIN-II | - |
dc.subject.keywordPlus | NEUROTENSIN RECEPTOR | - |
dc.subject.keywordPlus | MEMBRANE-PROTEINS | - |
dc.subject.keywordPlus | STRUCTURAL BASIS | - |
dc.subject.keywordPlus | INVERSE AGONISM | - |
dc.subject.keywordPlus | PICHIA-PASTORIS | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | COMPLEX | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordAuthor | G-protein coupled receptor | - |
dc.subject.keywordAuthor | Genetic modification | - |
dc.subject.keywordAuthor | Stabilization | - |
dc.subject.keywordAuthor | Antibody | - |
dc.subject.keywordAuthor | Detergent | - |
dc.subject.keywordAuthor | X-ray crystallography | - |
dc.identifier.url | https://www.sciencedirect.com/science/article/pii/S0005273613002484?via%3Dihub | - |
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