Activation of Nuclear Receptors: A Perspective from Structural Genomics
Crystal structures of more than two dozen different nuclear receptor ligand binding domains have defined a simple paradigm of receptor activation, in which agonist binding induces the activation function-2 (AF-2) helix to form a charge clamp for coactivator recruitment. Recent structural studies pre...
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| Veröffentlicht in: | Structure 2003-07, Vol.11 (7), p.741-746 |
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| creator | Li, Yong Lambert, Millard H Xu, H.Eric |
| description | Crystal structures of more than two dozen different nuclear receptor ligand binding domains have defined a simple paradigm of receptor activation, in which agonist binding induces the activation function-2 (AF-2) helix to form a charge clamp for coactivator recruitment. Recent structural studies present a surprising contrast. Activation of the mouse LRH-1 receptor is independent of a bound agonist despite its large ligand binding pocket, whereas the activation of the
Drosophila DHR38 receptor is dependent on ecdysteroids even though the receptor lacks a ligand binding pocket. These new findings shed light on the diverse structural mechanisms that nuclear receptors have evolved for activation, and have important implications in their respective signaling pathways. |
| doi_str_mv | 10.1016/S0969-2126(03)00133-3 |
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Drosophila DHR38 receptor is dependent on ecdysteroids even though the receptor lacks a ligand binding pocket. These new findings shed light on the diverse structural mechanisms that nuclear receptors have evolved for activation, and have important implications in their respective signaling pathways.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Drosophila</subject><subject>Genomics</subject><subject>Molecular Sequence Data</subject><subject>Receptors, Cytoplasmic and Nuclear - chemistry</subject><subject>Receptors, Cytoplasmic and Nuclear - genetics</subject><subject>Receptors, Cytoplasmic and Nuclear - physiology</subject><subject>Sequence Homology, Amino Acid</subject><issn>0969-2126</issn><issn>1878-4186</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtLAzEURoMoWqs_QZmV6GL0JplJM26kFK1CUbG6DmlyA5F5mcwU_Pf2pVtXd3P44J5DyBmFawpU3MyhEEXKKBOXwK8AKOcp3yMDKkcyzagU-2TwhxyR4xg_AYDlAIfkiDKZMeCjAZmOTeeXuvNNnTQuee5NiTokb2iw7ZoQb5Nx8oohtrjmMHGhqZJ5F3rT9UGXyRTrpvImnpADp8uIp7s7JB8P9--Tx3T2Mn2ajGep4ZnoUhTCci6Bo9VWS5cZa9CJQi4QM5o7Zgoncqllllko7CKnBplcaCcoSO0KPiQX2902NF89xk5VPhosS11j00c14lnOWc7_BamUkLN8vXi-A_tFhVa1wVc6fKtfRyvgbgvg6q-lx6Ci8VgbtD6srCjbeEVBrauoTRW1Vq6Aq00VxfkPOux-NA</recordid><startdate>20030701</startdate><enddate>20030701</enddate><creator>Li, Yong</creator><creator>Lambert, Millard H</creator><creator>Xu, H.Eric</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>20030701</creationdate><title>Activation of Nuclear Receptors: A Perspective from Structural Genomics</title><author>Li, Yong ; Lambert, Millard H ; Xu, H.Eric</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c346t-e66d33803edada8f4cdcef698bee415f2c9f658a844d09db51ce28baf6108af93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Drosophila</topic><topic>Genomics</topic><topic>Molecular Sequence Data</topic><topic>Receptors, Cytoplasmic and Nuclear - chemistry</topic><topic>Receptors, Cytoplasmic and Nuclear - genetics</topic><topic>Receptors, Cytoplasmic and Nuclear - physiology</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Yong</creatorcontrib><creatorcontrib>Lambert, Millard H</creatorcontrib><creatorcontrib>Xu, H.Eric</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Structure</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, Yong</au><au>Lambert, Millard H</au><au>Xu, H.Eric</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activation of Nuclear Receptors: A Perspective from Structural Genomics</atitle><jtitle>Structure</jtitle><addtitle>Structure</addtitle><date>2003-07-01</date><risdate>2003</risdate><volume>11</volume><issue>7</issue><spage>741</spage><epage>746</epage><pages>741-746</pages><issn>0969-2126</issn><eissn>1878-4186</eissn><abstract>Crystal structures of more than two dozen different nuclear receptor ligand binding domains have defined a simple paradigm of receptor activation, in which agonist binding induces the activation function-2 (AF-2) helix to form a charge clamp for coactivator recruitment. Recent structural studies present a surprising contrast. Activation of the mouse LRH-1 receptor is independent of a bound agonist despite its large ligand binding pocket, whereas the activation of the
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| source | MEDLINE; Cell Press Free Archives; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Animals Drosophila Genomics Molecular Sequence Data Receptors, Cytoplasmic and Nuclear - chemistry Receptors, Cytoplasmic and Nuclear - genetics Receptors, Cytoplasmic and Nuclear - physiology Sequence Homology, Amino Acid |
| title | Activation of Nuclear Receptors: A Perspective from Structural Genomics |
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