Structure of IL-22 Bound to Its High-Affinity IL-22R1 Chain
IL-22 is an IL-10 family cytokine that initiates innate immune responses against bacterial pathogens and contributes to immune disease. IL-22 biological activity is initiated by binding to a cell-surface complex composed of IL-22R1 and IL-10R2 receptor chains and further regulated by interactions wi...
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| Veröffentlicht in: | Structure 2008-09, Vol.16 (9), p.1333-1344 |
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| creator | Jones, Brandi C. Logsdon, Naomi J. Walter, Mark R. |
| description | IL-22 is an IL-10 family cytokine that initiates innate immune responses against bacterial pathogens and contributes to immune disease. IL-22 biological activity is initiated by binding to a cell-surface complex composed of IL-22R1 and IL-10R2 receptor chains and further regulated by interactions with a soluble binding protein, IL-22BP, which shares sequence similarity with an extracellular region of IL-22R1 (sIL-22R1). IL-22R1 also pairs with the IL-20R2 chain to induce IL-20 and IL-24 signaling. To define the molecular basis of these diverse interactions, we have determined the structure of the IL-22/sIL-22R1 complex. The structure, combined with homology modeling and surface plasmon resonance studies, defines the molecular basis for the distinct affinities and specificities of IL-22 and IL-10 receptor chains that regulate cellular targeting and signal transduction to elicit effective immune responses. |
| doi_str_mv | 10.1016/j.str.2008.06.005 |
| format | Article |
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(ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><description>IL-22 is an IL-10 family cytokine that initiates innate immune responses against bacterial pathogens and contributes to immune disease. IL-22 biological activity is initiated by binding to a cell-surface complex composed of IL-22R1 and IL-10R2 receptor chains and further regulated by interactions with a soluble binding protein, IL-22BP, which shares sequence similarity with an extracellular region of IL-22R1 (sIL-22R1). IL-22R1 also pairs with the IL-20R2 chain to induce IL-20 and IL-24 signaling. To define the molecular basis of these diverse interactions, we have determined the structure of the IL-22/sIL-22R1 complex. The structure, combined with homology modeling and surface plasmon resonance studies, defines the molecular basis for the distinct affinities and specificities of IL-22 and IL-10 receptor chains that regulate cellular targeting and signal transduction to elicit effective immune responses.</description><identifier>ISSN: 0969-2126</identifier><identifier>EISSN: 1878-4186</identifier><identifier>DOI: 10.1016/j.str.2008.06.005</identifier><identifier>PMID: 18599299</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; CHAINS ; Crystallography, X-Ray ; Humans ; Immunity, Cellular - physiology ; Interleukin-10 - chemistry ; Interleukin-10 - metabolism ; Interleukin-10 Receptor alpha Subunit - chemistry ; Interleukin-10 Receptor alpha Subunit - metabolism ; Interleukin-22 ; Interleukins - chemistry ; Interleukins - metabolism ; LYMPHOKINES ; MICROBIO ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; MOLIMMUNO ; PATHOGENS ; PHYSICS OF ELEMENTARY PARTICLES AND FIELDS ; PLASMONS ; PROTEIN ; Protein Binding ; Protein Structure, Quaternary ; Protein Transport - physiology ; Receptors, Interleukin - chemistry ; Receptors, Interleukin - metabolism ; RESONANCE ; Sequence Homology, Amino Acid ; Signal Transduction - immunology ; Signal Transduction - physiology ; SIMULATION ; Substrate Specificity</subject><ispartof>Structure, 2008-09, Vol.16 (9), p.1333-1344</ispartof><rights>2008 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c573t-3be2858c22680fc6be0c2e90a132a62e0836ef7ae105c36fb2cef7f60cf6d2373</citedby><cites>FETCH-LOGICAL-c573t-3be2858c22680fc6be0c2e90a132a62e0836ef7ae105c36fb2cef7f60cf6d2373</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0969212608002189$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18599299$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1006852$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Jones, Brandi C.</creatorcontrib><creatorcontrib>Logsdon, Naomi J.</creatorcontrib><creatorcontrib>Walter, Mark R.</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><title>Structure of IL-22 Bound to Its High-Affinity IL-22R1 Chain</title><title>Structure</title><addtitle>Structure</addtitle><description>IL-22 is an IL-10 family cytokine that initiates innate immune responses against bacterial pathogens and contributes to immune disease. IL-22 biological activity is initiated by binding to a cell-surface complex composed of IL-22R1 and IL-10R2 receptor chains and further regulated by interactions with a soluble binding protein, IL-22BP, which shares sequence similarity with an extracellular region of IL-22R1 (sIL-22R1). IL-22R1 also pairs with the IL-20R2 chain to induce IL-20 and IL-24 signaling. To define the molecular basis of these diverse interactions, we have determined the structure of the IL-22/sIL-22R1 complex. The structure, combined with homology modeling and surface plasmon resonance studies, defines the molecular basis for the distinct affinities and specificities of IL-22 and IL-10 receptor chains that regulate cellular targeting and signal transduction to elicit effective immune responses.</description><subject>Amino Acid Sequence</subject><subject>CHAINS</subject><subject>Crystallography, X-Ray</subject><subject>Humans</subject><subject>Immunity, Cellular - physiology</subject><subject>Interleukin-10 - chemistry</subject><subject>Interleukin-10 - metabolism</subject><subject>Interleukin-10 Receptor alpha Subunit - chemistry</subject><subject>Interleukin-10 Receptor alpha Subunit - metabolism</subject><subject>Interleukin-22</subject><subject>Interleukins - chemistry</subject><subject>Interleukins - metabolism</subject><subject>LYMPHOKINES</subject><subject>MICROBIO</subject><subject>Models, Biological</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>MOLIMMUNO</subject><subject>PATHOGENS</subject><subject>PHYSICS OF ELEMENTARY PARTICLES AND FIELDS</subject><subject>PLASMONS</subject><subject>PROTEIN</subject><subject>Protein Binding</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Transport - physiology</subject><subject>Receptors, Interleukin - chemistry</subject><subject>Receptors, Interleukin - metabolism</subject><subject>RESONANCE</subject><subject>Sequence Homology, Amino Acid</subject><subject>Signal Transduction - immunology</subject><subject>Signal Transduction - physiology</subject><subject>SIMULATION</subject><subject>Substrate Specificity</subject><issn>0969-2126</issn><issn>1878-4186</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkV2LEzEUhoMobl39Ad7I4IV3M56caTIJC8Ja1C0UBD-uwzRzsk1pJ2uSWdh_b8oUP270KoQ8503ePIy95NBw4PLtvkk5NgigGpANgHjEFlx1ql5yJR-zBWipa-QoL9izlPYAgALgKbvgSmiNWi_Y1dccJ5unSFVw1XpTI1bvwzQOVQ7VOqfqxt_u6mvn_Ojzwwx84dVq1_vxOXvi-kOiF-f1kn3_-OHb6qbefP60Xl1vaiu6NtftllAJZRGlAmfllsAiaeh5i71EAtVKcl1PHIRtpduiLVsnwTo5YNu1l-zdnHs3bY80WBpz7A_mLvpjHx9M6L35-2T0O3Mb7g3KtltyUQJezwEhZW-S9ZnszoZxJJsNB5BKYIHenG-J4cdEKZujT5YOh36kMCUjtVgCdvBfkGsh9RJVAfkM2hhSiuR-PZmDOQk0e1MEmpNAA9IUgWXm1Z9df0-cjRXgagao_Pi9p3jqQ6OlwcdTnSH4f8T_BF7VqVo</recordid><startdate>20080910</startdate><enddate>20080910</enddate><creator>Jones, Brandi C.</creator><creator>Logsdon, Naomi J.</creator><creator>Walter, Mark R.</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>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7T5</scope><scope>C1K</scope><scope>H94</scope><scope>7X8</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>20080910</creationdate><title>Structure of IL-22 Bound to Its High-Affinity IL-22R1 Chain</title><author>Jones, Brandi C. ; Logsdon, Naomi J. ; Walter, Mark R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c573t-3be2858c22680fc6be0c2e90a132a62e0836ef7ae105c36fb2cef7f60cf6d2373</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amino Acid Sequence</topic><topic>CHAINS</topic><topic>Crystallography, X-Ray</topic><topic>Humans</topic><topic>Immunity, Cellular - physiology</topic><topic>Interleukin-10 - chemistry</topic><topic>Interleukin-10 - metabolism</topic><topic>Interleukin-10 Receptor alpha Subunit - chemistry</topic><topic>Interleukin-10 Receptor alpha Subunit - metabolism</topic><topic>Interleukin-22</topic><topic>Interleukins - chemistry</topic><topic>Interleukins - metabolism</topic><topic>LYMPHOKINES</topic><topic>MICROBIO</topic><topic>Models, Biological</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>MOLIMMUNO</topic><topic>PATHOGENS</topic><topic>PHYSICS OF ELEMENTARY PARTICLES AND FIELDS</topic><topic>PLASMONS</topic><topic>PROTEIN</topic><topic>Protein Binding</topic><topic>Protein Structure, Quaternary</topic><topic>Protein Transport - physiology</topic><topic>Receptors, Interleukin - chemistry</topic><topic>Receptors, Interleukin - metabolism</topic><topic>RESONANCE</topic><topic>Sequence Homology, Amino Acid</topic><topic>Signal Transduction - immunology</topic><topic>Signal Transduction - physiology</topic><topic>SIMULATION</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jones, Brandi C.</creatorcontrib><creatorcontrib>Logsdon, Naomi J.</creatorcontrib><creatorcontrib>Walter, Mark R.</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</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>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Structure</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jones, Brandi C.</au><au>Logsdon, Naomi J.</au><au>Walter, Mark R.</au><aucorp>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure of IL-22 Bound to Its High-Affinity IL-22R1 Chain</atitle><jtitle>Structure</jtitle><addtitle>Structure</addtitle><date>2008-09-10</date><risdate>2008</risdate><volume>16</volume><issue>9</issue><spage>1333</spage><epage>1344</epage><pages>1333-1344</pages><issn>0969-2126</issn><eissn>1878-4186</eissn><abstract>IL-22 is an IL-10 family cytokine that initiates innate immune responses against bacterial pathogens and contributes to immune disease. IL-22 biological activity is initiated by binding to a cell-surface complex composed of IL-22R1 and IL-10R2 receptor chains and further regulated by interactions with a soluble binding protein, IL-22BP, which shares sequence similarity with an extracellular region of IL-22R1 (sIL-22R1). IL-22R1 also pairs with the IL-20R2 chain to induce IL-20 and IL-24 signaling. To define the molecular basis of these diverse interactions, we have determined the structure of the IL-22/sIL-22R1 complex. The structure, combined with homology modeling and surface plasmon resonance studies, defines the molecular basis for the distinct affinities and specificities of IL-22 and IL-10 receptor chains that regulate cellular targeting and signal transduction to elicit effective immune responses.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>18599299</pmid><doi>10.1016/j.str.2008.06.005</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Cell Press Free Archives; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence CHAINS Crystallography, X-Ray Humans Immunity, Cellular - physiology Interleukin-10 - chemistry Interleukin-10 - metabolism Interleukin-10 Receptor alpha Subunit - chemistry Interleukin-10 Receptor alpha Subunit - metabolism Interleukin-22 Interleukins - chemistry Interleukins - metabolism LYMPHOKINES MICROBIO Models, Biological Models, Molecular Molecular Sequence Data MOLIMMUNO PATHOGENS PHYSICS OF ELEMENTARY PARTICLES AND FIELDS PLASMONS PROTEIN Protein Binding Protein Structure, Quaternary Protein Transport - physiology Receptors, Interleukin - chemistry Receptors, Interleukin - metabolism RESONANCE Sequence Homology, Amino Acid Signal Transduction - immunology Signal Transduction - physiology SIMULATION Substrate Specificity |
| title | Structure of IL-22 Bound to Its High-Affinity IL-22R1 Chain |
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