A reinterpretation of the dimerization interface of the N‐terminal Domains of STATs
The crystal structures of the N‐terminal domain (N‐domain) and the core region of the STAT family of transcription factors have been determined previously. STATs can form cooperative higher order structures (tetramers or higher oligomers) while bound to DNA. The crystal packing in the STAT4 N‐domain...
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| Veröffentlicht in: | Protein science 2003-02, Vol.12 (2), p.361-365 |
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| container_title | Protein science |
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| creator | Chen, Xiaomin Bhandari, Rashna Vinkemeier, Uwe van den Akker, Focco Darnell, James E. Kuriyan, John |
| description | The crystal structures of the N‐terminal domain (N‐domain) and the core region of the STAT family of transcription factors have been determined previously. STATs can form cooperative higher order structures (tetramers or higher oligomers) while bound to DNA. The crystal packing in the STAT4 N‐domain crystal structure, determined at 1.5 Å resolution, suggests two alternate organizations of the N‐domain dimer. We now present the results of site directed mutagenesis of residues predicted to be involved at each dimer interface. Our results indicate that the dimer interface suggested earlier as being physiologically relevant is, in fact, unlikely to be so. Given the alternative model for the N‐domain dimer, the ability of the N‐domain to mediate interactions of two STAT dimers on DNA remains unchanged. |
| doi_str_mv | 10.1110/ps.0218903 |
| format | Article |
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STATs can form cooperative higher order structures (tetramers or higher oligomers) while bound to DNA. The crystal packing in the STAT4 N‐domain crystal structure, determined at 1.5 Å resolution, suggests two alternate organizations of the N‐domain dimer. We now present the results of site directed mutagenesis of residues predicted to be involved at each dimer interface. Our results indicate that the dimer interface suggested earlier as being physiologically relevant is, in fact, unlikely to be so. Given the alternative model for the N‐domain dimer, the ability of the N‐domain to mediate interactions of two STAT dimers on DNA remains unchanged.</description><identifier>ISSN: 0961-8368</identifier><identifier>EISSN: 1469-896X</identifier><identifier>DOI: 10.1110/ps.0218903</identifier><identifier>PMID: 12538899</identifier><language>eng</language><publisher>Bristol: Cold Spring Harbor Laboratory Press</publisher><subject>Binding Sites ; Circular Dichroism ; cooperative DNA binding ; Dimerization ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; For the Record ; Humans ; Models, Molecular ; Mutation - genetics ; Protein Binding ; Protein Structure, Tertiary ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; STAT ; STAT4 Transcription Factor ; Trans-Activators - chemistry ; Trans-Activators - genetics ; Trans-Activators - metabolism ; Ultracentrifugation</subject><ispartof>Protein science, 2003-02, Vol.12 (2), p.361-365</ispartof><rights>Copyright © 2003 The Protein Society</rights><rights>Copyright © Copyright 2003 The Protein Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4821-9a06a7a17424dfc45b619a9cac292d6005c2b0007806c6595452a83d1b2e82183</citedby><cites>FETCH-LOGICAL-c4821-9a06a7a17424dfc45b619a9cac292d6005c2b0007806c6595452a83d1b2e82183</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/PMC2312425/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2312425/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,1427,27901,27902,45550,45551,46384,46808,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12538899$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chen, Xiaomin</creatorcontrib><creatorcontrib>Bhandari, Rashna</creatorcontrib><creatorcontrib>Vinkemeier, Uwe</creatorcontrib><creatorcontrib>van den Akker, Focco</creatorcontrib><creatorcontrib>Darnell, James E.</creatorcontrib><creatorcontrib>Kuriyan, John</creatorcontrib><title>A reinterpretation of the dimerization interface of the N‐terminal Domains of STATs</title><title>Protein science</title><addtitle>Protein Sci</addtitle><description>The crystal structures of the N‐terminal domain (N‐domain) and the core region of the STAT family of transcription factors have been determined previously. STATs can form cooperative higher order structures (tetramers or higher oligomers) while bound to DNA. The crystal packing in the STAT4 N‐domain crystal structure, determined at 1.5 Å resolution, suggests two alternate organizations of the N‐domain dimer. We now present the results of site directed mutagenesis of residues predicted to be involved at each dimer interface. Our results indicate that the dimer interface suggested earlier as being physiologically relevant is, in fact, unlikely to be so. Given the alternative model for the N‐domain dimer, the ability of the N‐domain to mediate interactions of two STAT dimers on DNA remains unchanged.</description><subject>Binding Sites</subject><subject>Circular Dichroism</subject><subject>cooperative DNA binding</subject><subject>Dimerization</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>For the Record</subject><subject>Humans</subject><subject>Models, Molecular</subject><subject>Mutation - genetics</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>STAT</subject><subject>STAT4 Transcription Factor</subject><subject>Trans-Activators - chemistry</subject><subject>Trans-Activators - genetics</subject><subject>Trans-Activators - metabolism</subject><subject>Ultracentrifugation</subject><issn>0961-8368</issn><issn>1469-896X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1KAzEUhYMotlY3PoDMWpiam8ykyUYo9ReKFW3BXchkMjbS-SEZlbryEXxGn8SpU_82ri6c891zLwehfcB9AMBHle9jAlxguoG6EDERcsHuNlEXCwYhp4x30I73DxjjCAjdRh0gMeVciC6aDQNnbFEbVzlTq9qWRVBmQT03QWpz4-xLq30imdLmy716f31rpNwWahGclLmyhV95t9Ph1O-irUwtvNlbzx6anZ1ORxfheHJ-ORqOQx1xAqFQmKmBgkFEojTTUZwwEEpopYkgKcM41iRpvh5wzDSLRRzFRHGaQkJMs89pDx23udVjkptUm6J2aiErZ3PllrJUVv51CjuX9-WTJBRI1JTQQ4dtgHal985k37uA5apcWXm5LreBD35f-0HXbTYAtMCzXZjlP1Hy-mYCBFMG9AOnoYVR</recordid><startdate>200302</startdate><enddate>200302</enddate><creator>Chen, Xiaomin</creator><creator>Bhandari, Rashna</creator><creator>Vinkemeier, Uwe</creator><creator>van den Akker, Focco</creator><creator>Darnell, James E.</creator><creator>Kuriyan, John</creator><general>Cold Spring Harbor Laboratory Press</general><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>5PM</scope></search><sort><creationdate>200302</creationdate><title>A reinterpretation of the dimerization interface of the N‐terminal Domains of STATs</title><author>Chen, Xiaomin ; Bhandari, Rashna ; Vinkemeier, Uwe ; van den Akker, Focco ; Darnell, James E. ; Kuriyan, John</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4821-9a06a7a17424dfc45b619a9cac292d6005c2b0007806c6595452a83d1b2e82183</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Binding Sites</topic><topic>Circular Dichroism</topic><topic>cooperative DNA binding</topic><topic>Dimerization</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>For the Record</topic><topic>Humans</topic><topic>Models, Molecular</topic><topic>Mutation - genetics</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - metabolism</topic><topic>STAT</topic><topic>STAT4 Transcription Factor</topic><topic>Trans-Activators - chemistry</topic><topic>Trans-Activators - genetics</topic><topic>Trans-Activators - metabolism</topic><topic>Ultracentrifugation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chen, Xiaomin</creatorcontrib><creatorcontrib>Bhandari, Rashna</creatorcontrib><creatorcontrib>Vinkemeier, Uwe</creatorcontrib><creatorcontrib>van den Akker, Focco</creatorcontrib><creatorcontrib>Darnell, James E.</creatorcontrib><creatorcontrib>Kuriyan, John</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Protein science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chen, Xiaomin</au><au>Bhandari, Rashna</au><au>Vinkemeier, Uwe</au><au>van den Akker, Focco</au><au>Darnell, James E.</au><au>Kuriyan, John</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A reinterpretation of the dimerization interface of the N‐terminal Domains of STATs</atitle><jtitle>Protein science</jtitle><addtitle>Protein Sci</addtitle><date>2003-02</date><risdate>2003</risdate><volume>12</volume><issue>2</issue><spage>361</spage><epage>365</epage><pages>361-365</pages><issn>0961-8368</issn><eissn>1469-896X</eissn><abstract>The crystal structures of the N‐terminal domain (N‐domain) and the core region of the STAT family of transcription factors have been determined previously. STATs can form cooperative higher order structures (tetramers or higher oligomers) while bound to DNA. The crystal packing in the STAT4 N‐domain crystal structure, determined at 1.5 Å resolution, suggests two alternate organizations of the N‐domain dimer. We now present the results of site directed mutagenesis of residues predicted to be involved at each dimer interface. Our results indicate that the dimer interface suggested earlier as being physiologically relevant is, in fact, unlikely to be so. Given the alternative model for the N‐domain dimer, the ability of the N‐domain to mediate interactions of two STAT dimers on DNA remains unchanged.</abstract><cop>Bristol</cop><pub>Cold Spring Harbor Laboratory Press</pub><pmid>12538899</pmid><doi>10.1110/ps.0218903</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Binding Sites Circular Dichroism cooperative DNA binding Dimerization DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism For the Record Humans Models, Molecular Mutation - genetics Protein Binding Protein Structure, Tertiary Recombinant Proteins - chemistry Recombinant Proteins - metabolism STAT STAT4 Transcription Factor Trans-Activators - chemistry Trans-Activators - genetics Trans-Activators - metabolism Ultracentrifugation |
| title | A reinterpretation of the dimerization interface of the N‐terminal Domains of STATs |
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