Sequence and structural analysis of artemin based on ferritin: A comparative study
Artemia cysts can tolerate extreme environments, partly due to a heat-stable protein called artemin. According to previous studies, artemin shares structural similarity with ferritins. Actually, there is still no strong structural information about artemin three-dimensional (3-D) structure. In this...
Gespeichert in:
| Veröffentlicht in: | Biochimica et biophysica acta 2009-10, Vol.1794 (10), p.1407-1413 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1413 |
|---|---|
| container_issue | 10 |
| container_start_page | 1407 |
| container_title | Biochimica et biophysica acta |
| container_volume | 1794 |
| creator | Rasti, Behnam Shahangian, S. Shirin Sajedi, Reza H. Taghdir, Majid Hasannia, Sadegh Ranjbar, Bijan |
| description | Artemia cysts can tolerate extreme environments, partly due to a heat-stable protein called artemin. According to previous studies, artemin shares structural similarity with ferritins. Actually, there is still no strong structural information about artemin three-dimensional (3-D) structure. In this research, the artemin encoding gene from
Artemia urmiana was cloned and sequenced. A reliable 3-D model of artemin was initially built using ferritin as template and refined using Molecular Dynamic (MD) Simulation. It is interesting that the proposed model, confirmed by circular dichroism (CD), shows significant differences in secondary structure contents with ferritin. Three conserved regions (ferroxidase center, iron nucleation center and 3-fold channel) in ferritins, cooperating in iron-interaction, have been substantially changed in artemin. Analysis of C-terminal region of the model revealed its major role in preventing artemin from iron-binding due to some suitable interactions. Finally, it is concluded that significant differences between artemin and ferritin, both in conserved regions related to iron-interaction and three-dimensional structure, can justify their functional differences. |
| doi_str_mv | 10.1016/j.bbapap.2009.05.005 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1221138360</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1570963909001289</els_id><sourcerecordid>1221138360</sourcerecordid><originalsourceid>FETCH-LOGICAL-c393t-eaefdef96b0b3279e91855d2c3b69135778903761343369d610a8316e3d8ec383</originalsourceid><addsrcrecordid>eNp9kE1LJDEQhsOiqKv-g2XJSfbSbaXTSToeBJHdVRAEP84hnVRDhv7apFuYf2-GGdibp6qC562iHkJ-MCgZMHm9KdvWznYuKwBdgigBxDdyxhrVFKwW9VHuhYJCS65PyfeUNgAVKCVOyCnTdSN1rc_Iyyv-W3F0SO3oaVri6pY12j6Ptt-mkOjUURsXHMJIW5vQ02mkHcYYljDe0DvqpmG20S7hA3N-9dsLctzZPuHloZ6T9z-_3-4fiqfnv4_3d0-F45ovBVrsPHZattDySmnUrBHCV463UjMulGo0cCUZrzmX2ksGtuFMIvcNOt7wc3K13zvHKf-QFjOE5LDv7YjTmoxUksta1hn89SXIqoqxvFBCRus96uKUUsTOzDEMNm4NA7PTbjZmr93stBsQJmvPsZ-HC2s7oP8fOnjOwO0ewCzkI2A0yYWddh8iusX4KXx94RMQ_JR6</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1221138360</pqid></control><display><type>article</type><title>Sequence and structural analysis of artemin based on ferritin: A comparative study</title><source>MEDLINE</source><source>Access via ScienceDirect (Elsevier)</source><creator>Rasti, Behnam ; Shahangian, S. Shirin ; Sajedi, Reza H. ; Taghdir, Majid ; Hasannia, Sadegh ; Ranjbar, Bijan</creator><creatorcontrib>Rasti, Behnam ; Shahangian, S. Shirin ; Sajedi, Reza H. ; Taghdir, Majid ; Hasannia, Sadegh ; Ranjbar, Bijan</creatorcontrib><description>Artemia cysts can tolerate extreme environments, partly due to a heat-stable protein called artemin. According to previous studies, artemin shares structural similarity with ferritins. Actually, there is still no strong structural information about artemin three-dimensional (3-D) structure. In this research, the artemin encoding gene from
Artemia urmiana was cloned and sequenced. A reliable 3-D model of artemin was initially built using ferritin as template and refined using Molecular Dynamic (MD) Simulation. It is interesting that the proposed model, confirmed by circular dichroism (CD), shows significant differences in secondary structure contents with ferritin. Three conserved regions (ferroxidase center, iron nucleation center and 3-fold channel) in ferritins, cooperating in iron-interaction, have been substantially changed in artemin. Analysis of C-terminal region of the model revealed its major role in preventing artemin from iron-binding due to some suitable interactions. Finally, it is concluded that significant differences between artemin and ferritin, both in conserved regions related to iron-interaction and three-dimensional structure, can justify their functional differences.</description><identifier>ISSN: 1570-9639</identifier><identifier>ISSN: 0006-3002</identifier><identifier>EISSN: 1878-1454</identifier><identifier>DOI: 10.1016/j.bbapap.2009.05.005</identifier><identifier>PMID: 19486949</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Animals ; Artemia ; Artemia - chemistry ; Artemia - genetics ; Artemia urmiana ; Artemin ; Arthropod Proteins ; Base Sequence ; Ceruloplasmin - chemistry ; Ceruloplasmin - genetics ; Circular Dichroism ; Cloning, Molecular ; Conserved Sequence ; DNA Primers - genetics ; DNA, Complementary - genetics ; Ferritin ; Ferritins - chemistry ; Ferritins - genetics ; Homology modeling ; Invertebrate Hormones - chemistry ; Invertebrate Hormones - genetics ; Iron - chemistry ; Iron-Binding Proteins ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Secondary ; RNA-Binding Proteins - chemistry ; RNA-Binding Proteins - genetics ; Sequence Homology, Amino Acid ; Thermodynamics</subject><ispartof>Biochimica et biophysica acta, 2009-10, Vol.1794 (10), p.1407-1413</ispartof><rights>2009 Elsevier B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c393t-eaefdef96b0b3279e91855d2c3b69135778903761343369d610a8316e3d8ec383</citedby><cites>FETCH-LOGICAL-c393t-eaefdef96b0b3279e91855d2c3b69135778903761343369d610a8316e3d8ec383</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbapap.2009.05.005$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19486949$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rasti, Behnam</creatorcontrib><creatorcontrib>Shahangian, S. Shirin</creatorcontrib><creatorcontrib>Sajedi, Reza H.</creatorcontrib><creatorcontrib>Taghdir, Majid</creatorcontrib><creatorcontrib>Hasannia, Sadegh</creatorcontrib><creatorcontrib>Ranjbar, Bijan</creatorcontrib><title>Sequence and structural analysis of artemin based on ferritin: A comparative study</title><title>Biochimica et biophysica acta</title><addtitle>Biochim Biophys Acta</addtitle><description>Artemia cysts can tolerate extreme environments, partly due to a heat-stable protein called artemin. According to previous studies, artemin shares structural similarity with ferritins. Actually, there is still no strong structural information about artemin three-dimensional (3-D) structure. In this research, the artemin encoding gene from
Artemia urmiana was cloned and sequenced. A reliable 3-D model of artemin was initially built using ferritin as template and refined using Molecular Dynamic (MD) Simulation. It is interesting that the proposed model, confirmed by circular dichroism (CD), shows significant differences in secondary structure contents with ferritin. Three conserved regions (ferroxidase center, iron nucleation center and 3-fold channel) in ferritins, cooperating in iron-interaction, have been substantially changed in artemin. Analysis of C-terminal region of the model revealed its major role in preventing artemin from iron-binding due to some suitable interactions. Finally, it is concluded that significant differences between artemin and ferritin, both in conserved regions related to iron-interaction and three-dimensional structure, can justify their functional differences.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Artemia</subject><subject>Artemia - chemistry</subject><subject>Artemia - genetics</subject><subject>Artemia urmiana</subject><subject>Artemin</subject><subject>Arthropod Proteins</subject><subject>Base Sequence</subject><subject>Ceruloplasmin - chemistry</subject><subject>Ceruloplasmin - genetics</subject><subject>Circular Dichroism</subject><subject>Cloning, Molecular</subject><subject>Conserved Sequence</subject><subject>DNA Primers - genetics</subject><subject>DNA, Complementary - genetics</subject><subject>Ferritin</subject><subject>Ferritins - chemistry</subject><subject>Ferritins - genetics</subject><subject>Homology modeling</subject><subject>Invertebrate Hormones - chemistry</subject><subject>Invertebrate Hormones - genetics</subject><subject>Iron - chemistry</subject><subject>Iron-Binding Proteins</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><subject>RNA-Binding Proteins - chemistry</subject><subject>RNA-Binding Proteins - genetics</subject><subject>Sequence Homology, Amino Acid</subject><subject>Thermodynamics</subject><issn>1570-9639</issn><issn>0006-3002</issn><issn>1878-1454</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LJDEQhsOiqKv-g2XJSfbSbaXTSToeBJHdVRAEP84hnVRDhv7apFuYf2-GGdibp6qC562iHkJ-MCgZMHm9KdvWznYuKwBdgigBxDdyxhrVFKwW9VHuhYJCS65PyfeUNgAVKCVOyCnTdSN1rc_Iyyv-W3F0SO3oaVri6pY12j6Ptt-mkOjUURsXHMJIW5vQ02mkHcYYljDe0DvqpmG20S7hA3N-9dsLctzZPuHloZ6T9z-_3-4fiqfnv4_3d0-F45ovBVrsPHZattDySmnUrBHCV463UjMulGo0cCUZrzmX2ksGtuFMIvcNOt7wc3K13zvHKf-QFjOE5LDv7YjTmoxUksta1hn89SXIqoqxvFBCRus96uKUUsTOzDEMNm4NA7PTbjZmr93stBsQJmvPsZ-HC2s7oP8fOnjOwO0ewCzkI2A0yYWddh8iusX4KXx94RMQ_JR6</recordid><startdate>20091001</startdate><enddate>20091001</enddate><creator>Rasti, Behnam</creator><creator>Shahangian, S. Shirin</creator><creator>Sajedi, Reza H.</creator><creator>Taghdir, Majid</creator><creator>Hasannia, Sadegh</creator><creator>Ranjbar, Bijan</creator><general>Elsevier B.V</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>7QO</scope><scope>7TN</scope><scope>8FD</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>L.G</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20091001</creationdate><title>Sequence and structural analysis of artemin based on ferritin: A comparative study</title><author>Rasti, Behnam ; Shahangian, S. Shirin ; Sajedi, Reza H. ; Taghdir, Majid ; Hasannia, Sadegh ; Ranjbar, Bijan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c393t-eaefdef96b0b3279e91855d2c3b69135778903761343369d610a8316e3d8ec383</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Artemia</topic><topic>Artemia - chemistry</topic><topic>Artemia - genetics</topic><topic>Artemia urmiana</topic><topic>Artemin</topic><topic>Arthropod Proteins</topic><topic>Base Sequence</topic><topic>Ceruloplasmin - chemistry</topic><topic>Ceruloplasmin - genetics</topic><topic>Circular Dichroism</topic><topic>Cloning, Molecular</topic><topic>Conserved Sequence</topic><topic>DNA Primers - genetics</topic><topic>DNA, Complementary - genetics</topic><topic>Ferritin</topic><topic>Ferritins - chemistry</topic><topic>Ferritins - genetics</topic><topic>Homology modeling</topic><topic>Invertebrate Hormones - chemistry</topic><topic>Invertebrate Hormones - genetics</topic><topic>Iron - chemistry</topic><topic>Iron-Binding Proteins</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Protein Conformation</topic><topic>Protein Structure, Secondary</topic><topic>RNA-Binding Proteins - chemistry</topic><topic>RNA-Binding Proteins - genetics</topic><topic>Sequence Homology, Amino Acid</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rasti, Behnam</creatorcontrib><creatorcontrib>Shahangian, S. Shirin</creatorcontrib><creatorcontrib>Sajedi, Reza H.</creatorcontrib><creatorcontrib>Taghdir, Majid</creatorcontrib><creatorcontrib>Hasannia, Sadegh</creatorcontrib><creatorcontrib>Ranjbar, Bijan</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Oceanic Abstracts</collection><collection>Technology Research Database</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochimica et biophysica acta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rasti, Behnam</au><au>Shahangian, S. Shirin</au><au>Sajedi, Reza H.</au><au>Taghdir, Majid</au><au>Hasannia, Sadegh</au><au>Ranjbar, Bijan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sequence and structural analysis of artemin based on ferritin: A comparative study</atitle><jtitle>Biochimica et biophysica acta</jtitle><addtitle>Biochim Biophys Acta</addtitle><date>2009-10-01</date><risdate>2009</risdate><volume>1794</volume><issue>10</issue><spage>1407</spage><epage>1413</epage><pages>1407-1413</pages><issn>1570-9639</issn><issn>0006-3002</issn><eissn>1878-1454</eissn><abstract>Artemia cysts can tolerate extreme environments, partly due to a heat-stable protein called artemin. According to previous studies, artemin shares structural similarity with ferritins. Actually, there is still no strong structural information about artemin three-dimensional (3-D) structure. In this research, the artemin encoding gene from
Artemia urmiana was cloned and sequenced. A reliable 3-D model of artemin was initially built using ferritin as template and refined using Molecular Dynamic (MD) Simulation. It is interesting that the proposed model, confirmed by circular dichroism (CD), shows significant differences in secondary structure contents with ferritin. Three conserved regions (ferroxidase center, iron nucleation center and 3-fold channel) in ferritins, cooperating in iron-interaction, have been substantially changed in artemin. Analysis of C-terminal region of the model revealed its major role in preventing artemin from iron-binding due to some suitable interactions. Finally, it is concluded that significant differences between artemin and ferritin, both in conserved regions related to iron-interaction and three-dimensional structure, can justify their functional differences.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>19486949</pmid><doi>10.1016/j.bbapap.2009.05.005</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1570-9639 |
| ispartof | Biochimica et biophysica acta, 2009-10, Vol.1794 (10), p.1407-1413 |
| issn | 1570-9639 0006-3002 1878-1454 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1221138360 |
| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Amino Acid Sequence Animals Artemia Artemia - chemistry Artemia - genetics Artemia urmiana Artemin Arthropod Proteins Base Sequence Ceruloplasmin - chemistry Ceruloplasmin - genetics Circular Dichroism Cloning, Molecular Conserved Sequence DNA Primers - genetics DNA, Complementary - genetics Ferritin Ferritins - chemistry Ferritins - genetics Homology modeling Invertebrate Hormones - chemistry Invertebrate Hormones - genetics Iron - chemistry Iron-Binding Proteins Models, Molecular Molecular Sequence Data Protein Conformation Protein Structure, Secondary RNA-Binding Proteins - chemistry RNA-Binding Proteins - genetics Sequence Homology, Amino Acid Thermodynamics |
| title | Sequence and structural analysis of artemin based on ferritin: A comparative study |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-23T12%3A58%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=Sequence%20and%20structural%20analysis%20of%20artemin%20based%20on%20ferritin:%20A%20comparative%20study&rft.jtitle=Biochimica%20et%20biophysica%20acta&rft.au=Rasti,%20Behnam&rft.date=2009-10-01&rft.volume=1794&rft.issue=10&rft.spage=1407&rft.epage=1413&rft.pages=1407-1413&rft.issn=1570-9639&rft.eissn=1878-1454&rft_id=info:doi/10.1016/j.bbapap.2009.05.005&rft_dat=%3Cproquest_cross%3E1221138360%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=1221138360&rft_id=info:pmid/19486949&rft_els_id=S1570963909001289&rfr_iscdi=true |