Contributions of Zn(II)-binding to the structural stability of endostatin
Endostatin has a compact structure with a Zn(II)-binding site (His1, His3, His11, and Asp76) at the N-terminus. In this study, the effects of Zn(II)-binding on the folding and stability of recombinant human endostatin were studied. The results show that Zn(II)-binding largely stabilizes the structur...
Gespeichert in:
| Veröffentlicht in: | FEBS letters 2007-06, Vol.581 (16), p.3027-3032 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 3032 |
|---|---|
| container_issue | 16 |
| container_start_page | 3027 |
| container_title | FEBS letters |
| container_volume | 581 |
| creator | Han, Qing Fu, Yan Zhou, Hao He, Yingbo Luo, Yongzhang |
| description | Endostatin has a compact structure with a Zn(II)-binding site (His1, His3, His11, and Asp76) at the N-terminus. In this study, the effects of Zn(II)-binding on the folding and stability of recombinant human endostatin were studied. The results show that Zn(II)-binding largely stabilizes the structure of endostatin at physiological pH. Under some proteolytic conditions, Zn(II)-binding also contributes to the integrity of the N-terminus of endostatin, which is critical for endostatin to maintain a stable structure. Moreover, engineering an extra Zn(II)-binding peptide to the N-terminus of human endostatin makes this molecule more stable and cooperative in the presence of Zn(II). |
| doi_str_mv | 10.1016/j.febslet.2007.05.058 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_70610395</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0014579307005947</els_id><sourcerecordid>70610395</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5417-7a289a917778feb0566c83456f0762e99d3ea4a69c16aeb4f02dd7317b0713483</originalsourceid><addsrcrecordid>eNqNkU1v1DAQhi1ERbctPwGUE6KHLOP4Kz6hsmrpSpU4QC9cLMeZgFdZp9gOaP89jnYljlQayR7r9TszzxDyhsKaApUfdusBuzRiXjcAag2iRPuCrGirWM24bF-SFQDltVCanZOLlHZQ8pbqV-ScKsE5h3ZFtpsp5Oi7OfsppGoaqu_h_XZ7XXc-9D78qPJU5Z9YpRxnl-dox3K1nR99PixqDP1UHrIPV-RssGPC16fzkjze3X7b3NcPXz5vNzcPtROcqlrZptVWU6VUWyYAIaVrGRdyACUb1LpnaLmV2lFpseMDNH2vGFUdKMp4yy7Ju6PvU5x-zZiy2fvkcBxtwGlORoGkwLQoQnEUujilFHEwT9HvbTwYCmZhaHbmxNAsDA2IEkuBt6cCc7fH_t-vE7QiuD8K_vgRD89zNXe3n5qvy0KWfYACEJqrYvXxaIWF2G-P0STnMTjsfUSXTT_5_3T7F2xGmfs</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>70610395</pqid></control><display><type>article</type><title>Contributions of Zn(II)-binding to the structural stability of endostatin</title><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><source>Elsevier ScienceDirect Journals</source><source>Wiley Online Library Free Content</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>Han, Qing ; Fu, Yan ; Zhou, Hao ; He, Yingbo ; Luo, Yongzhang</creator><creatorcontrib>Han, Qing ; Fu, Yan ; Zhou, Hao ; He, Yingbo ; Luo, Yongzhang</creatorcontrib><description>Endostatin has a compact structure with a Zn(II)-binding site (His1, His3, His11, and Asp76) at the N-terminus. In this study, the effects of Zn(II)-binding on the folding and stability of recombinant human endostatin were studied. The results show that Zn(II)-binding largely stabilizes the structure of endostatin at physiological pH. Under some proteolytic conditions, Zn(II)-binding also contributes to the integrity of the N-terminus of endostatin, which is critical for endostatin to maintain a stable structure. Moreover, engineering an extra Zn(II)-binding peptide to the N-terminus of human endostatin makes this molecule more stable and cooperative in the presence of Zn(II).</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2007.05.058</identifier><identifier>PMID: 17544408</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Binding Sites ; Calorimetry, Differential Scanning ; circular dichroism ; differential scanning calorimetry ; DSC ; Endostatin ; Endostatins - chemistry ; Endostatins - metabolism ; fast protein liquid chromatography ; FluoZin-1, tripotassium salt ; FPLC ; GdmC1 ; Guanidine - pharmacology ; guanidine hydrochloride ; Humans ; Models, Molecular ; Peptide Fragments - chemical synthesis ; Peptide Fragments - chemistry ; Protein Binding ; Protein Denaturation - drug effects ; Protein Engineering ; Protein Folding ; Protein Structure, Secondary ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; Stability ; Trypsin - metabolism ; ZBP, Zn(II)-binding peptide ; ZBP-ES ; Zinc - metabolism ; Zn(II)-binding ; Zn(II)-binding peptide ; Zn(II)-binding peptide modified endostatin</subject><ispartof>FEBS letters, 2007-06, Vol.581 (16), p.3027-3032</ispartof><rights>2007 Federation of European Biochemical Societies</rights><rights>FEBS Letters 581 (2007) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5417-7a289a917778feb0566c83456f0762e99d3ea4a69c16aeb4f02dd7317b0713483</citedby><cites>FETCH-LOGICAL-c5417-7a289a917778feb0566c83456f0762e99d3ea4a69c16aeb4f02dd7317b0713483</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2007.05.058$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579307005947$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17544408$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Han, Qing</creatorcontrib><creatorcontrib>Fu, Yan</creatorcontrib><creatorcontrib>Zhou, Hao</creatorcontrib><creatorcontrib>He, Yingbo</creatorcontrib><creatorcontrib>Luo, Yongzhang</creatorcontrib><title>Contributions of Zn(II)-binding to the structural stability of endostatin</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Endostatin has a compact structure with a Zn(II)-binding site (His1, His3, His11, and Asp76) at the N-terminus. In this study, the effects of Zn(II)-binding on the folding and stability of recombinant human endostatin were studied. The results show that Zn(II)-binding largely stabilizes the structure of endostatin at physiological pH. Under some proteolytic conditions, Zn(II)-binding also contributes to the integrity of the N-terminus of endostatin, which is critical for endostatin to maintain a stable structure. Moreover, engineering an extra Zn(II)-binding peptide to the N-terminus of human endostatin makes this molecule more stable and cooperative in the presence of Zn(II).</description><subject>Binding Sites</subject><subject>Calorimetry, Differential Scanning</subject><subject>circular dichroism</subject><subject>differential scanning calorimetry</subject><subject>DSC</subject><subject>Endostatin</subject><subject>Endostatins - chemistry</subject><subject>Endostatins - metabolism</subject><subject>fast protein liquid chromatography</subject><subject>FluoZin-1, tripotassium salt</subject><subject>FPLC</subject><subject>GdmC1</subject><subject>Guanidine - pharmacology</subject><subject>guanidine hydrochloride</subject><subject>Humans</subject><subject>Models, Molecular</subject><subject>Peptide Fragments - chemical synthesis</subject><subject>Peptide Fragments - chemistry</subject><subject>Protein Binding</subject><subject>Protein Denaturation - drug effects</subject><subject>Protein Engineering</subject><subject>Protein Folding</subject><subject>Protein Structure, Secondary</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>Stability</subject><subject>Trypsin - metabolism</subject><subject>ZBP, Zn(II)-binding peptide</subject><subject>ZBP-ES</subject><subject>Zinc - metabolism</subject><subject>Zn(II)-binding</subject><subject>Zn(II)-binding peptide</subject><subject>Zn(II)-binding peptide modified endostatin</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1v1DAQhi1ERbctPwGUE6KHLOP4Kz6hsmrpSpU4QC9cLMeZgFdZp9gOaP89jnYljlQayR7r9TszzxDyhsKaApUfdusBuzRiXjcAag2iRPuCrGirWM24bF-SFQDltVCanZOLlHZQ8pbqV-ScKsE5h3ZFtpsp5Oi7OfsppGoaqu_h_XZ7XXc-9D78qPJU5Z9YpRxnl-dox3K1nR99PixqDP1UHrIPV-RssGPC16fzkjze3X7b3NcPXz5vNzcPtROcqlrZptVWU6VUWyYAIaVrGRdyACUb1LpnaLmV2lFpseMDNH2vGFUdKMp4yy7Ju6PvU5x-zZiy2fvkcBxtwGlORoGkwLQoQnEUujilFHEwT9HvbTwYCmZhaHbmxNAsDA2IEkuBt6cCc7fH_t-vE7QiuD8K_vgRD89zNXe3n5qvy0KWfYACEJqrYvXxaIWF2G-P0STnMTjsfUSXTT_5_3T7F2xGmfs</recordid><startdate>20070626</startdate><enddate>20070626</enddate><creator>Han, Qing</creator><creator>Fu, Yan</creator><creator>Zhou, Hao</creator><creator>He, Yingbo</creator><creator>Luo, Yongzhang</creator><general>Elsevier B.V</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>7X8</scope></search><sort><creationdate>20070626</creationdate><title>Contributions of Zn(II)-binding to the structural stability of endostatin</title><author>Han, Qing ; Fu, Yan ; Zhou, Hao ; He, Yingbo ; Luo, Yongzhang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5417-7a289a917778feb0566c83456f0762e99d3ea4a69c16aeb4f02dd7317b0713483</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Binding Sites</topic><topic>Calorimetry, Differential Scanning</topic><topic>circular dichroism</topic><topic>differential scanning calorimetry</topic><topic>DSC</topic><topic>Endostatin</topic><topic>Endostatins - chemistry</topic><topic>Endostatins - metabolism</topic><topic>fast protein liquid chromatography</topic><topic>FluoZin-1, tripotassium salt</topic><topic>FPLC</topic><topic>GdmC1</topic><topic>Guanidine - pharmacology</topic><topic>guanidine hydrochloride</topic><topic>Humans</topic><topic>Models, Molecular</topic><topic>Peptide Fragments - chemical synthesis</topic><topic>Peptide Fragments - chemistry</topic><topic>Protein Binding</topic><topic>Protein Denaturation - drug effects</topic><topic>Protein Engineering</topic><topic>Protein Folding</topic><topic>Protein Structure, Secondary</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - metabolism</topic><topic>Stability</topic><topic>Trypsin - metabolism</topic><topic>ZBP, Zn(II)-binding peptide</topic><topic>ZBP-ES</topic><topic>Zinc - metabolism</topic><topic>Zn(II)-binding</topic><topic>Zn(II)-binding peptide</topic><topic>Zn(II)-binding peptide modified endostatin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Han, Qing</creatorcontrib><creatorcontrib>Fu, Yan</creatorcontrib><creatorcontrib>Zhou, Hao</creatorcontrib><creatorcontrib>He, Yingbo</creatorcontrib><creatorcontrib>Luo, Yongzhang</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>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Han, Qing</au><au>Fu, Yan</au><au>Zhou, Hao</au><au>He, Yingbo</au><au>Luo, Yongzhang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Contributions of Zn(II)-binding to the structural stability of endostatin</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2007-06-26</date><risdate>2007</risdate><volume>581</volume><issue>16</issue><spage>3027</spage><epage>3032</epage><pages>3027-3032</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Endostatin has a compact structure with a Zn(II)-binding site (His1, His3, His11, and Asp76) at the N-terminus. In this study, the effects of Zn(II)-binding on the folding and stability of recombinant human endostatin were studied. The results show that Zn(II)-binding largely stabilizes the structure of endostatin at physiological pH. Under some proteolytic conditions, Zn(II)-binding also contributes to the integrity of the N-terminus of endostatin, which is critical for endostatin to maintain a stable structure. Moreover, engineering an extra Zn(II)-binding peptide to the N-terminus of human endostatin makes this molecule more stable and cooperative in the presence of Zn(II).</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>17544408</pmid><doi>10.1016/j.febslet.2007.05.058</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 2007-06, Vol.581 (16), p.3027-3032 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_70610395 |
| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Wiley Online Library Free Content; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Binding Sites Calorimetry, Differential Scanning circular dichroism differential scanning calorimetry DSC Endostatin Endostatins - chemistry Endostatins - metabolism fast protein liquid chromatography FluoZin-1, tripotassium salt FPLC GdmC1 Guanidine - pharmacology guanidine hydrochloride Humans Models, Molecular Peptide Fragments - chemical synthesis Peptide Fragments - chemistry Protein Binding Protein Denaturation - drug effects Protein Engineering Protein Folding Protein Structure, Secondary Recombinant Proteins - chemistry Recombinant Proteins - metabolism Stability Trypsin - metabolism ZBP, Zn(II)-binding peptide ZBP-ES Zinc - metabolism Zn(II)-binding Zn(II)-binding peptide Zn(II)-binding peptide modified endostatin |
| title | Contributions of Zn(II)-binding to the structural stability of endostatin |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-03T13%3A16%3A48IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Contributions%20of%20Zn(II)-binding%20to%20the%20structural%20stability%20of%20endostatin&rft.jtitle=FEBS%20letters&rft.au=Han,%20Qing&rft.date=2007-06-26&rft.volume=581&rft.issue=16&rft.spage=3027&rft.epage=3032&rft.pages=3027-3032&rft.issn=0014-5793&rft.eissn=1873-3468&rft_id=info:doi/10.1016/j.febslet.2007.05.058&rft_dat=%3Cproquest_cross%3E70610395%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=70610395&rft_id=info:pmid/17544408&rft_els_id=S0014579307005947&rfr_iscdi=true |