Common and distinct mechanisms of activation of rhodopsin and other G protein-coupled receptors
Detailed and systematic examination of high-resolution structural data is a rational strategy for understanding the function of biological macromolecules. G protein-coupled receptors (GPCRs) are an exceptionally valuable superfamily of proteins for such analysis. The most intriguing question is how...
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| Veröffentlicht in: | Scientific reports 2013-05, Vol.3 (1), p.1844-1844, Article 1844 |
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| creator | Nakamura, Sumire Itabashi, Takeshi Ogawa, Daisuke Okada, Tetsuji |
| description | Detailed and systematic examination of high-resolution structural data is a rational strategy for understanding the function of biological macromolecules. G protein-coupled receptors (GPCRs) are an exceptionally valuable superfamily of proteins for such analysis. The most intriguing question is how a variety of extracellular stimuli evoke structural changes in the intracellular surface of the receptors. The recent active-like crystal structures of GPCRs provide information for uncovering common and distinct mechanisms of light-induced and ligand-induced activation. Based on systematic structural alignment, we have analyzed 3 receptors (rhodopsin, β
2
adrenergic receptor, adenosine A
2A
receptor) and demonstrate that the extracellular movement of helix VI is significantly different between rhodopsin and the other 2 receptors and that the extracellular side of helix III exhibits distinct features in the 3 receptors. These findings not only emphasize the specialization of rhodopsin as a photoreceptor but also provide insights into the mechanism leading to rearrangement of helix VI. |
| doi_str_mv | 10.1038/srep01844 |
| format | Article |
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2
adrenergic receptor, adenosine A
2A
receptor) and demonstrate that the extracellular movement of helix VI is significantly different between rhodopsin and the other 2 receptors and that the extracellular side of helix III exhibits distinct features in the 3 receptors. These findings not only emphasize the specialization of rhodopsin as a photoreceptor but also provide insights into the mechanism leading to rearrangement of helix VI.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep01844</identifier><identifier>PMID: 23677071</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/114 ; 631/45/535 ; 631/535/1266 ; 631/57 ; Adrenergic receptors ; Cytoplasm ; G protein-coupled receptors ; Humanities and Social Sciences ; Humans ; Ligands ; Light effects ; Macromolecules ; Models, Molecular ; multidisciplinary ; Protein Conformation ; Protein Structure, Secondary ; Proteins ; Receptor mechanisms ; Receptor, Adenosine A2A - chemistry ; Receptor, Adenosine A2A - metabolism ; Receptors, Adrenergic, beta-2 - chemistry ; Receptors, Adrenergic, beta-2 - metabolism ; Rhodopsin ; Rhodopsin - chemistry ; Rhodopsin - metabolism ; Science ; Specialization</subject><ispartof>Scientific reports, 2013-05, Vol.3 (1), p.1844-1844, Article 1844</ispartof><rights>The Author(s) 2013</rights><rights>Copyright Nature Publishing Group May 2013</rights><rights>Copyright © 2013, Macmillan Publishers Limited. All rights reserved 2013 Macmillan Publishers Limited. All rights reserved</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c504t-ec0f14d7721ceb7453c0c026a216cc3e678f6f75acac0bea9fb3ef14554c0fe83</citedby><cites>FETCH-LOGICAL-c504t-ec0f14d7721ceb7453c0c026a216cc3e678f6f75acac0bea9fb3ef14554c0fe83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3654499/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3654499/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,27901,27902,41096,42165,51551,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23677071$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nakamura, Sumire</creatorcontrib><creatorcontrib>Itabashi, Takeshi</creatorcontrib><creatorcontrib>Ogawa, Daisuke</creatorcontrib><creatorcontrib>Okada, Tetsuji</creatorcontrib><title>Common and distinct mechanisms of activation of rhodopsin and other G protein-coupled receptors</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Detailed and systematic examination of high-resolution structural data is a rational strategy for understanding the function of biological macromolecules. G protein-coupled receptors (GPCRs) are an exceptionally valuable superfamily of proteins for such analysis. The most intriguing question is how a variety of extracellular stimuli evoke structural changes in the intracellular surface of the receptors. The recent active-like crystal structures of GPCRs provide information for uncovering common and distinct mechanisms of light-induced and ligand-induced activation. Based on systematic structural alignment, we have analyzed 3 receptors (rhodopsin, β
2
adrenergic receptor, adenosine A
2A
receptor) and demonstrate that the extracellular movement of helix VI is significantly different between rhodopsin and the other 2 receptors and that the extracellular side of helix III exhibits distinct features in the 3 receptors. These findings not only emphasize the specialization of rhodopsin as a photoreceptor but also provide insights into the mechanism leading to rearrangement of helix VI.</description><subject>631/114</subject><subject>631/45/535</subject><subject>631/535/1266</subject><subject>631/57</subject><subject>Adrenergic receptors</subject><subject>Cytoplasm</subject><subject>G protein-coupled receptors</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>Ligands</subject><subject>Light effects</subject><subject>Macromolecules</subject><subject>Models, Molecular</subject><subject>multidisciplinary</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Receptor mechanisms</subject><subject>Receptor, Adenosine A2A - chemistry</subject><subject>Receptor, Adenosine A2A - metabolism</subject><subject>Receptors, Adrenergic, beta-2 - chemistry</subject><subject>Receptors, Adrenergic, beta-2 - metabolism</subject><subject>Rhodopsin</subject><subject>Rhodopsin - chemistry</subject><subject>Rhodopsin - metabolism</subject><subject>Science</subject><subject>Specialization</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNplkV9rFTEQxUNR2tL2wS8gC76osDV_N5sXoVy0CgVf9Dnkzs72puwma5It-O1NufVy1bwkw_zOmQmHkFeMXjMq-g854UJZL-UJOedUqpYLzl8cvc_IVc4PtB7FjWTmlJxx0WlNNTsndhPnOYbGhaEZfC4-QGlmhJ0LPs-5iWPjoPhHV3ylapV2cYhL9ntJLDtMzW2zpFjQhxbiukw4NAkBlxJTviQvRzdlvHq-L8iPz5--b760d99uv25u7lpQVJYWgY5MDlpzBrjVUgmgQHnnOOsABHa6H7tRKwcO6BadGbcCq0IpWZXYiwvyce-7rNsZB8BQkpvskvzs0i8bnbd_d4Lf2fv4aEWnpDSmGrx9Nkjx54q52NlnwGlyAeOaLRNKUMmkeZr15h_0Ia4p1O9Z1hstuTE9rdS7PQUp5hrSeFiGUfuUnD0kV9nXx9sfyD85VeD9Hsi1Fe4xHY38z-03uxqkiw</recordid><startdate>20130515</startdate><enddate>20130515</enddate><creator>Nakamura, Sumire</creator><creator>Itabashi, Takeshi</creator><creator>Ogawa, Daisuke</creator><creator>Okada, Tetsuji</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20130515</creationdate><title>Common and distinct mechanisms of activation of rhodopsin and other G protein-coupled receptors</title><author>Nakamura, Sumire ; Itabashi, Takeshi ; Ogawa, Daisuke ; Okada, Tetsuji</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c504t-ec0f14d7721ceb7453c0c026a216cc3e678f6f75acac0bea9fb3ef14554c0fe83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>631/114</topic><topic>631/45/535</topic><topic>631/535/1266</topic><topic>631/57</topic><topic>Adrenergic receptors</topic><topic>Cytoplasm</topic><topic>G protein-coupled receptors</topic><topic>Humanities and Social Sciences</topic><topic>Humans</topic><topic>Ligands</topic><topic>Light effects</topic><topic>Macromolecules</topic><topic>Models, Molecular</topic><topic>multidisciplinary</topic><topic>Protein Conformation</topic><topic>Protein Structure, Secondary</topic><topic>Proteins</topic><topic>Receptor mechanisms</topic><topic>Receptor, Adenosine A2A - chemistry</topic><topic>Receptor, Adenosine A2A - metabolism</topic><topic>Receptors, Adrenergic, beta-2 - chemistry</topic><topic>Receptors, Adrenergic, beta-2 - metabolism</topic><topic>Rhodopsin</topic><topic>Rhodopsin - chemistry</topic><topic>Rhodopsin - metabolism</topic><topic>Science</topic><topic>Specialization</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nakamura, Sumire</creatorcontrib><creatorcontrib>Itabashi, Takeshi</creatorcontrib><creatorcontrib>Ogawa, Daisuke</creatorcontrib><creatorcontrib>Okada, Tetsuji</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nakamura, Sumire</au><au>Itabashi, Takeshi</au><au>Ogawa, Daisuke</au><au>Okada, Tetsuji</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Common and distinct mechanisms of activation of rhodopsin and other G protein-coupled receptors</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2013-05-15</date><risdate>2013</risdate><volume>3</volume><issue>1</issue><spage>1844</spage><epage>1844</epage><pages>1844-1844</pages><artnum>1844</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Detailed and systematic examination of high-resolution structural data is a rational strategy for understanding the function of biological macromolecules. 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2
adrenergic receptor, adenosine A
2A
receptor) and demonstrate that the extracellular movement of helix VI is significantly different between rhodopsin and the other 2 receptors and that the extracellular side of helix III exhibits distinct features in the 3 receptors. These findings not only emphasize the specialization of rhodopsin as a photoreceptor but also provide insights into the mechanism leading to rearrangement of helix VI.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>23677071</pmid><doi>10.1038/srep01844</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/114 631/45/535 631/535/1266 631/57 Adrenergic receptors Cytoplasm G protein-coupled receptors Humanities and Social Sciences Humans Ligands Light effects Macromolecules Models, Molecular multidisciplinary Protein Conformation Protein Structure, Secondary Proteins Receptor mechanisms Receptor, Adenosine A2A - chemistry Receptor, Adenosine A2A - metabolism Receptors, Adrenergic, beta-2 - chemistry Receptors, Adrenergic, beta-2 - metabolism Rhodopsin Rhodopsin - chemistry Rhodopsin - metabolism Science Specialization |
| title | Common and distinct mechanisms of activation of rhodopsin and other G protein-coupled receptors |
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