Molecular Modeling of Insect Ferritins
Amino acid sequences of ferritin subunits from three orders of insects (Diptera: Drosophila and Aedes; Lepidoptera: Calpodes and Manduca; and Homoptera: Nilaparvata) were obtained from the public database, and analyzed using structural modeling algorithms. Pattern recognition analysis identifies ce...
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| Veröffentlicht in: | In silico biology 2002, Vol.2 (1), p.S31-S44 |
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| container_title | In silico biology |
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| creator | Pham, Daphne Q.-D. |
| description | Amino acid sequences of ferritin subunits from three orders of
insects (Diptera: Drosophila and Aedes; Lepidoptera: Calpodes and Manduca; and
Homoptera: Nilaparvata) were obtained from the public database, and analyzed
using structural modeling algorithms. Pattern recognition analysis
identifies cell attachment, glycosylation, myristoylation, microbody targeting,
phosphorylation, cAMP/cGMP dependent, protein kinase C, casein kinase, and
tyrosine kinase sites in these subunits. The modeling analyses
suggest that the insect heavy-chain homologues are similar to their vertebrate
analogues and retain all active sites, including the ferroxidase
center. On the contrary, the insect light-chain homologues are
different from their vertebrate counterparts, and show none of these
features.Five á-helices were located in the Dipteran and Lepidopteran,
but not in Homopteran ferritin subunits. |
| doi_str_mv | 10.3233/ISB-00023 |
| format | Article |
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insects (Diptera: Drosophila and Aedes; Lepidoptera: Calpodes and Manduca; and
Homoptera: Nilaparvata) were obtained from the public database, and analyzed
using structural modeling algorithms. Pattern recognition analysis
identifies cell attachment, glycosylation, myristoylation, microbody targeting,
phosphorylation, cAMP/cGMP dependent, protein kinase C, casein kinase, and
tyrosine kinase sites in these subunits. The modeling analyses
suggest that the insect heavy-chain homologues are similar to their vertebrate
analogues and retain all active sites, including the ferroxidase
center. On the contrary, the insect light-chain homologues are
different from their vertebrate counterparts, and show none of these
features.Five á-helices were located in the Dipteran and Lepidopteran,
but not in Homopteran ferritin subunits.</description><identifier>ISSN: 1386-6338</identifier><identifier>EISSN: 1434-3207</identifier><identifier>DOI: 10.3233/ISB-00023</identifier><identifier>PMID: 11808875</identifier><language>eng</language><publisher>London, England: SAGE Publications</publisher><subject>Aedes ; Amino Acid Sequence ; Animals ; Calpodes ; Diptera ; Drosophila ; Ferritins - chemistry ; Ferritins - metabolism ; Homoptera ; Insect Proteins - chemistry ; Insect Proteins - metabolism ; Lepidoptera ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Processing, Post-Translational ; Sequence Homology, Amino Acid ; Vertebrates</subject><ispartof>In silico biology, 2002, Vol.2 (1), p.S31-S44</ispartof><rights>IOS Press. All rights reserved</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4010,27900,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11808875$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pham, Daphne Q.-D.</creatorcontrib><title>Molecular Modeling of Insect Ferritins</title><title>In silico biology</title><addtitle>In Silico Biol</addtitle><description>Amino acid sequences of ferritin subunits from three orders of
insects (Diptera: Drosophila and Aedes; Lepidoptera: Calpodes and Manduca; and
Homoptera: Nilaparvata) were obtained from the public database, and analyzed
using structural modeling algorithms. Pattern recognition analysis
identifies cell attachment, glycosylation, myristoylation, microbody targeting,
phosphorylation, cAMP/cGMP dependent, protein kinase C, casein kinase, and
tyrosine kinase sites in these subunits. The modeling analyses
suggest that the insect heavy-chain homologues are similar to their vertebrate
analogues and retain all active sites, including the ferroxidase
center. On the contrary, the insect light-chain homologues are
different from their vertebrate counterparts, and show none of these
features.Five á-helices were located in the Dipteran and Lepidopteran,
but not in Homopteran ferritin subunits.</description><subject>Aedes</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Calpodes</subject><subject>Diptera</subject><subject>Drosophila</subject><subject>Ferritins - chemistry</subject><subject>Ferritins - metabolism</subject><subject>Homoptera</subject><subject>Insect Proteins - chemistry</subject><subject>Insect Proteins - metabolism</subject><subject>Lepidoptera</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Protein Conformation</subject><subject>Protein Processing, Post-Translational</subject><subject>Sequence Homology, Amino Acid</subject><subject>Vertebrates</subject><issn>1386-6338</issn><issn>1434-3207</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkDFPwzAQhS0EoqUw8AdQpm4Bn8-1nRGqFiK1YgBmy0kuVao0CXYy8O8JUMTIdE-nT096H2PXwG9RIN6lLw8x51zgCZuCRBmj4Pp0zGhUrBDNhF2EsB8RI4U8ZxMAw43Riymbb9ua8qF2Ptq2BdVVs4vaMkqbQHkfrcn7qq-acMnOSlcHujreGXtbr16XT_Hm-TFd3m_iDozs4yxLdAmEgFg6g6AycuQWWmjuykQK7owCWSSKxoeRUslCc-IqyXPQWZngjM1_ejvfvg8UenuoQk517Rpqh2A1SAFK839BSNTCGFAjeHMEh-xAhe18dXD-w_4q-GsKbkd23w6-GRda4PbLrR3d2m-3-AnFbmYr</recordid><startdate>2002</startdate><enddate>2002</enddate><creator>Pham, Daphne Q.-D.</creator><general>SAGE Publications</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QO</scope><scope>7SS</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>2002</creationdate><title>Molecular Modeling of Insect Ferritins</title><author>Pham, Daphne Q.-D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p184t-bb97f1e3133fa8316beaea57270af9420a8614d96e70a84464d70e069cc17bf93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Aedes</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Calpodes</topic><topic>Diptera</topic><topic>Drosophila</topic><topic>Ferritins - chemistry</topic><topic>Ferritins - metabolism</topic><topic>Homoptera</topic><topic>Insect Proteins - chemistry</topic><topic>Insect Proteins - metabolism</topic><topic>Lepidoptera</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Protein Conformation</topic><topic>Protein Processing, Post-Translational</topic><topic>Sequence Homology, Amino Acid</topic><topic>Vertebrates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pham, Daphne Q.-D.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Biotechnology Research Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>In silico biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pham, Daphne Q.-D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular Modeling of Insect Ferritins</atitle><jtitle>In silico biology</jtitle><addtitle>In Silico Biol</addtitle><date>2002</date><risdate>2002</risdate><volume>2</volume><issue>1</issue><spage>S31</spage><epage>S44</epage><pages>S31-S44</pages><issn>1386-6338</issn><eissn>1434-3207</eissn><abstract>Amino acid sequences of ferritin subunits from three orders of
insects (Diptera: Drosophila and Aedes; Lepidoptera: Calpodes and Manduca; and
Homoptera: Nilaparvata) were obtained from the public database, and analyzed
using structural modeling algorithms. Pattern recognition analysis
identifies cell attachment, glycosylation, myristoylation, microbody targeting,
phosphorylation, cAMP/cGMP dependent, protein kinase C, casein kinase, and
tyrosine kinase sites in these subunits. The modeling analyses
suggest that the insect heavy-chain homologues are similar to their vertebrate
analogues and retain all active sites, including the ferroxidase
center. On the contrary, the insect light-chain homologues are
different from their vertebrate counterparts, and show none of these
features.Five á-helices were located in the Dipteran and Lepidopteran,
but not in Homopteran ferritin subunits.</abstract><cop>London, England</cop><pub>SAGE Publications</pub><pmid>11808875</pmid><doi>10.3233/ISB-00023</doi></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1386-6338 |
| ispartof | In silico biology, 2002, Vol.2 (1), p.S31-S44 |
| issn | 1386-6338 1434-3207 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_71421670 |
| source | MEDLINE; Free Full-Text Journals in Chemistry |
| subjects | Aedes Amino Acid Sequence Animals Calpodes Diptera Drosophila Ferritins - chemistry Ferritins - metabolism Homoptera Insect Proteins - chemistry Insect Proteins - metabolism Lepidoptera Models, Molecular Molecular Sequence Data Protein Conformation Protein Processing, Post-Translational Sequence Homology, Amino Acid Vertebrates |
| title | Molecular Modeling of Insect Ferritins |
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