Death Domain Assembly Mechanism Revealed by Crystal Structure of the Oligomeric PIDDosome Core Complex
Proteins of the death domain (DD) superfamily mediate assembly of oligomeric signaling complexes for the activation of caspases and kinases via unknown mechanisms. Here we report the crystal structure of the PIDD DD and RAIDD DD complex, which forms the core of the caspase-2-activating complex PIDDo...
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| Veröffentlicht in: | Cell 2007-02, Vol.128 (3), p.533-546 |
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| creator | Park, Hyun Ho Logette, Emmanuelle Raunser, Stefan Cuenin, Solange Walz, Thomas Tschopp, Jurg Wu, Hao |
| description | Proteins of the death domain (DD) superfamily mediate assembly of oligomeric signaling complexes for the activation of caspases and kinases via unknown mechanisms. Here we report the crystal structure of the PIDD DD and RAIDD DD complex, which forms the core of the caspase-2-activating complex PIDDosome. Although RAIDD DD and PIDD DD are monomers, they assemble into a complex that comprises seven RAIDD DDs and five PIDD DDs. Despite the use of an asymmetric assembly mechanism, all DDs in the complex are in quasi-equivalent environments. The structure provided eight unique asymmetric interfaces, which can be classified into three types. These three types of interactions together cover a majority of the DD surface. Mutagenesis on almost all interfaces leads to disruption of the assembly, resulting in defective caspase-2 activation. The three types of interactions may represent most, if not all, modes of interactions in the DD superfamily for assembling complexes of different stoichiometry. |
| doi_str_mv | 10.1016/j.cell.2007.01.019 |
| format | Article |
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(ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><description>Proteins of the death domain (DD) superfamily mediate assembly of oligomeric signaling complexes for the activation of caspases and kinases via unknown mechanisms. Here we report the crystal structure of the PIDD DD and RAIDD DD complex, which forms the core of the caspase-2-activating complex PIDDosome. Although RAIDD DD and PIDD DD are monomers, they assemble into a complex that comprises seven RAIDD DDs and five PIDD DDs. Despite the use of an asymmetric assembly mechanism, all DDs in the complex are in quasi-equivalent environments. The structure provided eight unique asymmetric interfaces, which can be classified into three types. These three types of interactions together cover a majority of the DD surface. Mutagenesis on almost all interfaces leads to disruption of the assembly, resulting in defective caspase-2 activation. The three types of interactions may represent most, if not all, modes of interactions in the DD superfamily for assembling complexes of different stoichiometry.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/j.cell.2007.01.019</identifier><identifier>PMID: 17289572</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Caspase 2 - metabolism ; CELLBIO ; CELLIMMUNO ; CRADD Signaling Adaptor Protein - chemistry ; CRADD Signaling Adaptor Protein - genetics ; CRADD Signaling Adaptor Protein - metabolism ; Crystallography, X-Ray ; Death Domain Receptor Signaling Adaptor Proteins - chemistry ; Death Domain Receptor Signaling Adaptor Proteins - genetics ; Death Domain Receptor Signaling Adaptor Proteins - metabolism ; Models, Molecular ; Molecular Sequence Data ; Multiprotein Complexes - metabolism ; Mutagenesis, Site-Directed ; Protein Conformation ; Protein Structure, Tertiary ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism</subject><ispartof>Cell, 2007-02, Vol.128 (3), p.533-546</ispartof><rights>2007 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c546t-dfd15481b7553b3b5deaaed1b94bbd21f1ff57cb8800a9585bf0fbae323ae3173</citedby><cites>FETCH-LOGICAL-c546t-dfd15481b7553b3b5deaaed1b94bbd21f1ff57cb8800a9585bf0fbae323ae3173</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S009286740700116X$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17289572$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1223972$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Park, Hyun Ho</creatorcontrib><creatorcontrib>Logette, Emmanuelle</creatorcontrib><creatorcontrib>Raunser, Stefan</creatorcontrib><creatorcontrib>Cuenin, Solange</creatorcontrib><creatorcontrib>Walz, Thomas</creatorcontrib><creatorcontrib>Tschopp, Jurg</creatorcontrib><creatorcontrib>Wu, Hao</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><title>Death Domain Assembly Mechanism Revealed by Crystal Structure of the Oligomeric PIDDosome Core Complex</title><title>Cell</title><addtitle>Cell</addtitle><description>Proteins of the death domain (DD) superfamily mediate assembly of oligomeric signaling complexes for the activation of caspases and kinases via unknown mechanisms. Here we report the crystal structure of the PIDD DD and RAIDD DD complex, which forms the core of the caspase-2-activating complex PIDDosome. Although RAIDD DD and PIDD DD are monomers, they assemble into a complex that comprises seven RAIDD DDs and five PIDD DDs. Despite the use of an asymmetric assembly mechanism, all DDs in the complex are in quasi-equivalent environments. The structure provided eight unique asymmetric interfaces, which can be classified into three types. These three types of interactions together cover a majority of the DD surface. Mutagenesis on almost all interfaces leads to disruption of the assembly, resulting in defective caspase-2 activation. The three types of interactions may represent most, if not all, modes of interactions in the DD superfamily for assembling complexes of different stoichiometry.</description><subject>Amino Acid Sequence</subject><subject>Caspase 2 - metabolism</subject><subject>CELLBIO</subject><subject>CELLIMMUNO</subject><subject>CRADD Signaling Adaptor Protein - chemistry</subject><subject>CRADD Signaling Adaptor Protein - genetics</subject><subject>CRADD Signaling Adaptor Protein - metabolism</subject><subject>Crystallography, X-Ray</subject><subject>Death Domain Receptor Signaling Adaptor Proteins - chemistry</subject><subject>Death Domain Receptor Signaling Adaptor Proteins - genetics</subject><subject>Death Domain Receptor Signaling Adaptor Proteins - metabolism</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Multiprotein Complexes - metabolism</subject><subject>Mutagenesis, Site-Directed</subject><subject>Protein Conformation</subject><subject>Protein Structure, Tertiary</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9UdtqGzEQFaWhcd3-QB-K6Pu6knbl3YVSCHYvgZSUXp6FLiNbRrsykmzqv-m39MuixaFJXwrDDMOcOWeYg9ArShaU0OXb3UKD9wtGSLsgtET_BM0o6duqoS17imaE9Kzqlm1ziZ6ntCOEdJzzZ-iyjLuet2yGNmuQeYvXYZBuxFcpwaD8CX8BvZWjSwP-BkeQHgxWJ7yKp5Slx99zPOh8iICDxXkLf37fercJA0Sn8dfr9Tqk0uBViFMa9h5-vUAXVvoEL-_rHP38-OHH6nN1c_vpenV1U2neLHNlrKG86ahqOa9VrbgBKcFQ1TdKGUYttZa3WnUdIbLnHVeWWCWhZnVJtK3n6P2Zd39QAxgNY47Si310g4wnEaQT_05GtxWbcBSsJ11daObozZkgpOxE0i6XV-gwjqCzoIzVfTuB2BmkY0gpgv0rQImYvBE7MXkjJm8EoSX6svT68WkPK_dmFMC7MwDKg44O4iQPowbj4qRugvsf_x0FGKN-</recordid><startdate>20070209</startdate><enddate>20070209</enddate><creator>Park, Hyun Ho</creator><creator>Logette, Emmanuelle</creator><creator>Raunser, Stefan</creator><creator>Cuenin, Solange</creator><creator>Walz, Thomas</creator><creator>Tschopp, Jurg</creator><creator>Wu, Hao</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>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>20070209</creationdate><title>Death Domain Assembly Mechanism Revealed by Crystal Structure of the Oligomeric PIDDosome Core Complex</title><author>Park, Hyun Ho ; Logette, Emmanuelle ; Raunser, Stefan ; Cuenin, Solange ; Walz, Thomas ; Tschopp, Jurg ; Wu, Hao</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c546t-dfd15481b7553b3b5deaaed1b94bbd21f1ff57cb8800a9585bf0fbae323ae3173</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Amino Acid Sequence</topic><topic>Caspase 2 - metabolism</topic><topic>CELLBIO</topic><topic>CELLIMMUNO</topic><topic>CRADD Signaling Adaptor Protein - chemistry</topic><topic>CRADD Signaling Adaptor Protein - genetics</topic><topic>CRADD Signaling Adaptor Protein - metabolism</topic><topic>Crystallography, X-Ray</topic><topic>Death Domain Receptor Signaling Adaptor Proteins - chemistry</topic><topic>Death Domain Receptor Signaling Adaptor Proteins - genetics</topic><topic>Death Domain Receptor Signaling Adaptor Proteins - metabolism</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Multiprotein Complexes - metabolism</topic><topic>Mutagenesis, Site-Directed</topic><topic>Protein Conformation</topic><topic>Protein Structure, Tertiary</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Park, Hyun Ho</creatorcontrib><creatorcontrib>Logette, Emmanuelle</creatorcontrib><creatorcontrib>Raunser, Stefan</creatorcontrib><creatorcontrib>Cuenin, Solange</creatorcontrib><creatorcontrib>Walz, Thomas</creatorcontrib><creatorcontrib>Tschopp, Jurg</creatorcontrib><creatorcontrib>Wu, Hao</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>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Park, Hyun Ho</au><au>Logette, Emmanuelle</au><au>Raunser, Stefan</au><au>Cuenin, Solange</au><au>Walz, Thomas</au><au>Tschopp, Jurg</au><au>Wu, Hao</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>Death Domain Assembly Mechanism Revealed by Crystal Structure of the Oligomeric PIDDosome Core Complex</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>2007-02-09</date><risdate>2007</risdate><volume>128</volume><issue>3</issue><spage>533</spage><epage>546</epage><pages>533-546</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>Proteins of the death domain (DD) superfamily mediate assembly of oligomeric signaling complexes for the activation of caspases and kinases via unknown mechanisms. Here we report the crystal structure of the PIDD DD and RAIDD DD complex, which forms the core of the caspase-2-activating complex PIDDosome. Although RAIDD DD and PIDD DD are monomers, they assemble into a complex that comprises seven RAIDD DDs and five PIDD DDs. Despite the use of an asymmetric assembly mechanism, all DDs in the complex are in quasi-equivalent environments. The structure provided eight unique asymmetric interfaces, which can be classified into three types. These three types of interactions together cover a majority of the DD surface. Mutagenesis on almost all interfaces leads to disruption of the assembly, resulting in defective caspase-2 activation. The three types of interactions may represent most, if not all, modes of interactions in the DD superfamily for assembling complexes of different stoichiometry.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17289572</pmid><doi>10.1016/j.cell.2007.01.019</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Caspase 2 - metabolism CELLBIO CELLIMMUNO CRADD Signaling Adaptor Protein - chemistry CRADD Signaling Adaptor Protein - genetics CRADD Signaling Adaptor Protein - metabolism Crystallography, X-Ray Death Domain Receptor Signaling Adaptor Proteins - chemistry Death Domain Receptor Signaling Adaptor Proteins - genetics Death Domain Receptor Signaling Adaptor Proteins - metabolism Models, Molecular Molecular Sequence Data Multiprotein Complexes - metabolism Mutagenesis, Site-Directed Protein Conformation Protein Structure, Tertiary Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism |
| title | Death Domain Assembly Mechanism Revealed by Crystal Structure of the Oligomeric PIDDosome Core Complex |
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