The Crystal Structure of a TL/CD8[alpha][alpha] Complex at 2.1 Å Resolution: Implications for Modulation of T Cell Activation and Memory
TL is a nonclassical MHC class I molecule that modulates T cell activation through relatively high-affinity interaction with CD8αα. To investigate how the TL/CD8αα interaction influences TCR signaling, we characterized the structure of the TL/CD8αα complex using X-ray crystallography. Unlike antigen...
Gespeichert in:
| Veröffentlicht in: | Immunity 2003-02, Vol.18 (2), p.205 |
|---|---|
| Hauptverfasser: | , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | |
|---|---|
| container_issue | 2 |
| container_start_page | 205 |
| container_title | Immunity |
| container_volume | 18 |
| creator | Liu, Yiwei Xiong, Yi Naidenko, Olga V Liu, Jin-huan Zhang, Rongguang Joachimiak, Andrzej Kronenberg, Mitchell Cheroutre, Hilde Reinherz, Ellis L Wang, Jia-huai |
| description | TL is a nonclassical MHC class I molecule that modulates T cell activation through relatively high-affinity interaction with CD8αα. To investigate how the TL/CD8αα interaction influences TCR signaling, we characterized the structure of the TL/CD8αα complex using X-ray crystallography. Unlike antigen-presenting molecules, the TL antigen-binding groove is occluded by specific conformational changes. This feature eliminates antigen presentation, severely hampers direct TCR recognition, and prevents TL from participating in the TCR activation complex. At the same time, the TL/CD8αα interaction is strengthened through subtle structure changes in the TL α3 domain. Thus, TL functions to sequester and redirect CD8αα away from the TCR, modifying lck-dependent signaling. |
| doi_str_mv | 10.1016/S1074-7613(03)00027-X |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_osti_</sourceid><recordid>TN_cdi_proquest_journals_1504191203</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>3236422191</sourcerecordid><originalsourceid>FETCH-LOGICAL-o543-c9438e1a9bee8712ca5682b356a023921fd2b1d3816350bdc0d7d5da194ed6033</originalsourceid><addsrcrecordid>eNotjt1KwzAYhoMoOKuXIEQ80YNu35ekaXMo9RcKguuBIFLSJGMbtZlNCnoBXpk35mQ7et6Dh4eXkHOEKQLK2RwhF2kukV8BvwYAlqevB2SCoPJUYAGH_3uvHJOTENYAKDIFE1LVS0fL4TtE3dF5HEYTx8FRv6Ca1tWsvC3edLdZ6vc9aOk_Np37ojpSNkX6-0NfXPDdGFe-PyVHC90Fd7ZnQur7u7p8TKvnh6fypkp9JnhqlOCFQ61a54ocmdGZLFjLM6mBccVwYVmLlhcoeQatNWBzm1mNSjgrgfOEXOyyPsRVE8wqOrM0vu-diY2SyLZSQi53zmbwn6MLsVn7cei3rxrMQKBCti39AbZ5WeY</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1504191203</pqid></control><display><type>article</type><title>The Crystal Structure of a TL/CD8[alpha][alpha] Complex at 2.1 Å Resolution: Implications for Modulation of T Cell Activation and Memory</title><source>Cell Press Free Archives</source><source>ScienceDirect Journals (5 years ago - present)</source><source>EZB-FREE-00999 freely available EZB journals</source><creator>Liu, Yiwei ; Xiong, Yi ; Naidenko, Olga V ; Liu, Jin-huan ; Zhang, Rongguang ; Joachimiak, Andrzej ; Kronenberg, Mitchell ; Cheroutre, Hilde ; Reinherz, Ellis L ; Wang, Jia-huai</creator><creatorcontrib>Liu, Yiwei ; Xiong, Yi ; Naidenko, Olga V ; Liu, Jin-huan ; Zhang, Rongguang ; Joachimiak, Andrzej ; Kronenberg, Mitchell ; Cheroutre, Hilde ; Reinherz, Ellis L ; Wang, Jia-huai ; Argonne National Lab. (ANL), Argonne, IL (United States)</creatorcontrib><description>TL is a nonclassical MHC class I molecule that modulates T cell activation through relatively high-affinity interaction with CD8αα. To investigate how the TL/CD8αα interaction influences TCR signaling, we characterized the structure of the TL/CD8αα complex using X-ray crystallography. Unlike antigen-presenting molecules, the TL antigen-binding groove is occluded by specific conformational changes. This feature eliminates antigen presentation, severely hampers direct TCR recognition, and prevents TL from participating in the TCR activation complex. At the same time, the TL/CD8αα interaction is strengthened through subtle structure changes in the TL α3 domain. Thus, TL functions to sequester and redirect CD8αα away from the TCR, modifying lck-dependent signaling.</description><identifier>ISSN: 1074-7613</identifier><identifier>EISSN: 1097-4180</identifier><identifier>DOI: 10.1016/S1074-7613(03)00027-X</identifier><language>eng</language><publisher>Cambridge: Elsevier Limited</publisher><subject>60 APPLIED LIFE SCIENCES ; ANTIGENS ; CONFORMATIONAL CHANGES ; CRYSTAL STRUCTURE ; CRYSTALLOGRAPHY ; GLYCOPROTEINS ; INTERACTIONS ; LYMPHOCYTES ; MATERIALS SCIENCE ; Medical research ; MODULATION ; MOLECULES ; Peptides ; Proteins ; RECEPTORS ; RESOLUTION</subject><ispartof>Immunity, 2003-02, Vol.18 (2), p.205</ispartof><rights>Copyright Elsevier Limited Feb 2003</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.osti.gov/biblio/961260$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Liu, Yiwei</creatorcontrib><creatorcontrib>Xiong, Yi</creatorcontrib><creatorcontrib>Naidenko, Olga V</creatorcontrib><creatorcontrib>Liu, Jin-huan</creatorcontrib><creatorcontrib>Zhang, Rongguang</creatorcontrib><creatorcontrib>Joachimiak, Andrzej</creatorcontrib><creatorcontrib>Kronenberg, Mitchell</creatorcontrib><creatorcontrib>Cheroutre, Hilde</creatorcontrib><creatorcontrib>Reinherz, Ellis L</creatorcontrib><creatorcontrib>Wang, Jia-huai</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States)</creatorcontrib><title>The Crystal Structure of a TL/CD8[alpha][alpha] Complex at 2.1 Å Resolution: Implications for Modulation of T Cell Activation and Memory</title><title>Immunity</title><description>TL is a nonclassical MHC class I molecule that modulates T cell activation through relatively high-affinity interaction with CD8αα. To investigate how the TL/CD8αα interaction influences TCR signaling, we characterized the structure of the TL/CD8αα complex using X-ray crystallography. Unlike antigen-presenting molecules, the TL antigen-binding groove is occluded by specific conformational changes. This feature eliminates antigen presentation, severely hampers direct TCR recognition, and prevents TL from participating in the TCR activation complex. At the same time, the TL/CD8αα interaction is strengthened through subtle structure changes in the TL α3 domain. Thus, TL functions to sequester and redirect CD8αα away from the TCR, modifying lck-dependent signaling.</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>ANTIGENS</subject><subject>CONFORMATIONAL CHANGES</subject><subject>CRYSTAL STRUCTURE</subject><subject>CRYSTALLOGRAPHY</subject><subject>GLYCOPROTEINS</subject><subject>INTERACTIONS</subject><subject>LYMPHOCYTES</subject><subject>MATERIALS SCIENCE</subject><subject>Medical research</subject><subject>MODULATION</subject><subject>MOLECULES</subject><subject>Peptides</subject><subject>Proteins</subject><subject>RECEPTORS</subject><subject>RESOLUTION</subject><issn>1074-7613</issn><issn>1097-4180</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><recordid>eNotjt1KwzAYhoMoOKuXIEQ80YNu35ekaXMo9RcKguuBIFLSJGMbtZlNCnoBXpk35mQ7et6Dh4eXkHOEKQLK2RwhF2kukV8BvwYAlqevB2SCoPJUYAGH_3uvHJOTENYAKDIFE1LVS0fL4TtE3dF5HEYTx8FRv6Ca1tWsvC3edLdZ6vc9aOk_Np37ojpSNkX6-0NfXPDdGFe-PyVHC90Fd7ZnQur7u7p8TKvnh6fypkp9JnhqlOCFQ61a54ocmdGZLFjLM6mBccVwYVmLlhcoeQatNWBzm1mNSjgrgfOEXOyyPsRVE8wqOrM0vu-diY2SyLZSQi53zmbwn6MLsVn7cei3rxrMQKBCti39AbZ5WeY</recordid><startdate>20030201</startdate><enddate>20030201</enddate><creator>Liu, Yiwei</creator><creator>Xiong, Yi</creator><creator>Naidenko, Olga V</creator><creator>Liu, Jin-huan</creator><creator>Zhang, Rongguang</creator><creator>Joachimiak, Andrzej</creator><creator>Kronenberg, Mitchell</creator><creator>Cheroutre, Hilde</creator><creator>Reinherz, Ellis L</creator><creator>Wang, Jia-huai</creator><general>Elsevier Limited</general><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>NAPCQ</scope><scope>P64</scope><scope>RC3</scope><scope>OTOTI</scope></search><sort><creationdate>20030201</creationdate><title>The Crystal Structure of a TL/CD8[alpha][alpha] Complex at 2.1 Å Resolution</title><author>Liu, Yiwei ; Xiong, Yi ; Naidenko, Olga V ; Liu, Jin-huan ; Zhang, Rongguang ; Joachimiak, Andrzej ; Kronenberg, Mitchell ; Cheroutre, Hilde ; Reinherz, Ellis L ; Wang, Jia-huai</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-o543-c9438e1a9bee8712ca5682b356a023921fd2b1d3816350bdc0d7d5da194ed6033</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>ANTIGENS</topic><topic>CONFORMATIONAL CHANGES</topic><topic>CRYSTAL STRUCTURE</topic><topic>CRYSTALLOGRAPHY</topic><topic>GLYCOPROTEINS</topic><topic>INTERACTIONS</topic><topic>LYMPHOCYTES</topic><topic>MATERIALS SCIENCE</topic><topic>Medical research</topic><topic>MODULATION</topic><topic>MOLECULES</topic><topic>Peptides</topic><topic>Proteins</topic><topic>RECEPTORS</topic><topic>RESOLUTION</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liu, Yiwei</creatorcontrib><creatorcontrib>Xiong, Yi</creatorcontrib><creatorcontrib>Naidenko, Olga V</creatorcontrib><creatorcontrib>Liu, Jin-huan</creatorcontrib><creatorcontrib>Zhang, Rongguang</creatorcontrib><creatorcontrib>Joachimiak, Andrzej</creatorcontrib><creatorcontrib>Kronenberg, Mitchell</creatorcontrib><creatorcontrib>Cheroutre, Hilde</creatorcontrib><creatorcontrib>Reinherz, Ellis L</creatorcontrib><creatorcontrib>Wang, Jia-huai</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States)</creatorcontrib><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Nursing & Allied Health Premium</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>OSTI.GOV</collection><jtitle>Immunity</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liu, Yiwei</au><au>Xiong, Yi</au><au>Naidenko, Olga V</au><au>Liu, Jin-huan</au><au>Zhang, Rongguang</au><au>Joachimiak, Andrzej</au><au>Kronenberg, Mitchell</au><au>Cheroutre, Hilde</au><au>Reinherz, Ellis L</au><au>Wang, Jia-huai</au><aucorp>Argonne National Lab. (ANL), Argonne, IL (United States)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Crystal Structure of a TL/CD8[alpha][alpha] Complex at 2.1 Å Resolution: Implications for Modulation of T Cell Activation and Memory</atitle><jtitle>Immunity</jtitle><date>2003-02-01</date><risdate>2003</risdate><volume>18</volume><issue>2</issue><spage>205</spage><pages>205-</pages><issn>1074-7613</issn><eissn>1097-4180</eissn><abstract>TL is a nonclassical MHC class I molecule that modulates T cell activation through relatively high-affinity interaction with CD8αα. To investigate how the TL/CD8αα interaction influences TCR signaling, we characterized the structure of the TL/CD8αα complex using X-ray crystallography. Unlike antigen-presenting molecules, the TL antigen-binding groove is occluded by specific conformational changes. This feature eliminates antigen presentation, severely hampers direct TCR recognition, and prevents TL from participating in the TCR activation complex. At the same time, the TL/CD8αα interaction is strengthened through subtle structure changes in the TL α3 domain. Thus, TL functions to sequester and redirect CD8αα away from the TCR, modifying lck-dependent signaling.</abstract><cop>Cambridge</cop><pub>Elsevier Limited</pub><doi>10.1016/S1074-7613(03)00027-X</doi></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1074-7613 |
| ispartof | Immunity, 2003-02, Vol.18 (2), p.205 |
| issn | 1074-7613 1097-4180 |
| language | eng |
| recordid | cdi_proquest_journals_1504191203 |
| source | Cell Press Free Archives; ScienceDirect Journals (5 years ago - present); EZB-FREE-00999 freely available EZB journals |
| subjects | 60 APPLIED LIFE SCIENCES ANTIGENS CONFORMATIONAL CHANGES CRYSTAL STRUCTURE CRYSTALLOGRAPHY GLYCOPROTEINS INTERACTIONS LYMPHOCYTES MATERIALS SCIENCE Medical research MODULATION MOLECULES Peptides Proteins RECEPTORS RESOLUTION |
| title | The Crystal Structure of a TL/CD8[alpha][alpha] Complex at 2.1 Å Resolution: Implications for Modulation of T Cell Activation and Memory |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-07T12%3A06%3A11IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_osti_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20Crystal%20Structure%20of%20a%20TL/CD8%5Balpha%5D%5Balpha%5D%20Complex%20at%202.1%20%C3%85%20Resolution:%20Implications%20for%20Modulation%20of%20T%20Cell%20Activation%20and%20Memory&rft.jtitle=Immunity&rft.au=Liu,%20Yiwei&rft.aucorp=Argonne%20National%20Lab.%20(ANL),%20Argonne,%20IL%20(United%20States)&rft.date=2003-02-01&rft.volume=18&rft.issue=2&rft.spage=205&rft.pages=205-&rft.issn=1074-7613&rft.eissn=1097-4180&rft_id=info:doi/10.1016/S1074-7613(03)00027-X&rft_dat=%3Cproquest_osti_%3E3236422191%3C/proquest_osti_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1504191203&rft_id=info:pmid/&rfr_iscdi=true |