Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser


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KANG, Yanyong, X. Edward ZHOU, Xiang GAO, Yuanzheng HE, Kay DIEDERICHS, Eric H. XU, 2015. Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser. In: Nature. 523(7562), pp. 561-567. ISSN 0028-0836. eISSN 1476-4687. Available under: doi: 10.1038/nature14656

@article{Kang2015Cryst-31788, title={Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser}, year={2015}, doi={10.1038/nature14656}, number={7562}, volume={523}, issn={0028-0836}, journal={Nature}, pages={561--567}, author={Kang, Yanyong and Zhou, X. Edward and Gao, Xiang and He, Yuanzheng and Diederichs, Kay and Xu, Eric H.} }

<rdf:RDF xmlns:dcterms="" xmlns:dc="" xmlns:rdf="" xmlns:bibo="" xmlns:dspace="" xmlns:foaf="" xmlns:void="" xmlns:xsd="" > <rdf:Description rdf:about=""> <dc:creator>Zhou, X. Edward</dc:creator> <dcterms:title>Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser</dcterms:title> <dcterms:hasPart rdf:resource=""/> <dc:creator>Xu, Eric H.</dc:creator> <dspace:isPartOfCollection rdf:resource=""/> <dc:rights>terms-of-use</dc:rights> <dcterms:issued>2015</dcterms:issued> <dc:creator>Gao, Xiang</dc:creator> <dc:creator>He, Yuanzheng</dc:creator> <dc:contributor>Zhou, X. Edward</dc:contributor> <dc:contributor>Diederichs, Kay</dc:contributor> <dcterms:available rdf:datatype="">2015-09-21T11:10:30Z</dcterms:available> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dc:contributor>Gao, Xiang</dc:contributor> <bibo:uri rdf:resource=""/> <dcterms:abstract xml:lang="eng">G-protein-coupled receptors (GPCRs) signal primarily through G proteins or arrestins. Arrestin binding to GPCRs blocks G protein interaction and redirects signalling to numerous G-protein-independent pathways. Here we report the crystal structure of a constitutively active form of human rhodopsin bound to a pre-activated form of the mouse visual arrestin, determined by serial femtosecond X-ray laser crystallography. Together with extensive biochemical and mutagenesis data, the structure reveals an overall architecture of the rhodopsin–arrestin assembly in which rhodopsin uses distinct structural elements, including transmembrane helix 7 and helix 8, to recruit arrestin. Correspondingly, arrestin adopts the pre-activated conformation, with a ~20° rotation between the amino and carboxy domains, which opens up a cleft in arrestin to accommodate a short helix formed by the second intracellular loop of rhodopsin. This structure provides a basis for understanding GPCR-mediated arrestin-biased signalling and demonstrates the power of X-ray lasers for advancing the frontiers of structural biology.</dcterms:abstract> <dcterms:rights rdf:resource=""/> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:contributor>Kang, Yanyong</dc:contributor> <dc:contributor>Xu, Eric H.</dc:contributor> <dspace:hasBitstream rdf:resource=""/> <dc:contributor>He, Yuanzheng</dc:contributor> <dc:date rdf:datatype="">2015-09-21T11:10:30Z</dc:date> <dc:language>eng</dc:language> <dcterms:isPartOf rdf:resource=""/> <dc:creator>Diederichs, Kay</dc:creator> <dc:creator>Kang, Yanyong</dc:creator> </rdf:Description> </rdf:RDF>

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