Secondary structure and 3D homology modeling of grass carp ( Ctenopharyngodon idellus) major histocompatibility complex class I molecules
No information to date is available on the structure of fish major histocompatibility complex (MHC) class I and β2-microglobulin (β2m) proteins. In the present study, grass carp ( Ctenopharyngodon idellus) MHC class I ( Ctid-MHC I) and β 2-microglobulin ( Ctid-β2m) genes were expressed as soluble ma...
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| Veröffentlicht in: | Protein expression and purification 2007, Vol.51 (1), p.120-125 |
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| creator | Fang Hao, Hui Li, Xin-Sheng Gao, Feng-Shan Xue Wu, Wen Xia, Chun |
| description | No information to date is available on the structure of fish major histocompatibility complex (MHC) class I and β2-microglobulin (β2m) proteins. In the present study, grass carp (
Ctenopharyngodon idellus) MHC class I (
Ctid-MHC I) and β
2-microglobulin (
Ctid-β2m) genes were expressed as soluble maltose binding protein (MBP)-proteins and purified in a pMAL-p2X/
Escherichia coli TB1 system. The expressed proteins were purified on amylase affinity columns followed by DEAE–Sepharose. The purified products were identified by Western blotting with anti-MBP polyclonal antibodies. The MBP-
Ctid-MHC I and MBP-
Ctid-β2m were cleaved separately with Factor Xa, mixed together and purified on DEAE–Sepharose. The secondary structures were analyzed by circular dichroism (CD) spectrophotometry. The three-dimensional (3D) structure of their peptide-binding domain (PBD) was modeled based sequence homology. The sequence lengths of the α-helix, β-sheet, turn, and random coil in the
Ctid-MHC I protein were 79
aa, 75
aa, 20
aa, and 99
aa, respectively. In the 97
aa of
Ctid-β2m, the contents of the α-helix, β-sheet, turn, and random coil were 0
aa, 41
aa, 12
aa, and 44
aa, respectively. The
Ctid-β2m protein displayed a typical β-sheet. Homology modeling of the
Ctid-MHC I and
Ctid-β2m proteins demonstrated similarities with the structure of human MHC class I proteins. |
| doi_str_mv | 10.1016/j.pep.2006.08.003 |
| format | Article |
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Ctenopharyngodon idellus) MHC class I (
Ctid-MHC I) and β
2-microglobulin (
Ctid-β2m) genes were expressed as soluble maltose binding protein (MBP)-proteins and purified in a pMAL-p2X/
Escherichia coli TB1 system. The expressed proteins were purified on amylase affinity columns followed by DEAE–Sepharose. The purified products were identified by Western blotting with anti-MBP polyclonal antibodies. The MBP-
Ctid-MHC I and MBP-
Ctid-β2m were cleaved separately with Factor Xa, mixed together and purified on DEAE–Sepharose. The secondary structures were analyzed by circular dichroism (CD) spectrophotometry. The three-dimensional (3D) structure of their peptide-binding domain (PBD) was modeled based sequence homology. The sequence lengths of the α-helix, β-sheet, turn, and random coil in the
Ctid-MHC I protein were 79
aa, 75
aa, 20
aa, and 99
aa, respectively. In the 97
aa of
Ctid-β2m, the contents of the α-helix, β-sheet, turn, and random coil were 0
aa, 41
aa, 12
aa, and 44
aa, respectively. The
Ctid-β2m protein displayed a typical β-sheet. Homology modeling of the
Ctid-MHC I and
Ctid-β2m proteins demonstrated similarities with the structure of human MHC class I proteins.</description><identifier>ISSN: 1046-5928</identifier><identifier>EISSN: 1096-0279</identifier><identifier>DOI: 10.1016/j.pep.2006.08.003</identifier><identifier>PMID: 17005417</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; beta 2-Microglobulin - chemistry ; beta 2-Microglobulin - isolation & purification ; Carps - immunology ; Circular Dichroism ; Circular dichroism spectrum ; Ctenopharyngodon idella ; Escherichia coli ; Genetic Vectors ; Grass carp ; Histocompatibility Antigens Class I - chemistry ; Histocompatibility Antigens Class I - isolation & purification ; Homology modeling ; MHC I ; Models, Molecular ; Protein Structure, Secondary ; Recombinant Fusion Proteins - biosynthesis ; Recombinant Fusion Proteins - chemistry ; Secondary structure ; β 2-microglobulin</subject><ispartof>Protein expression and purification, 2007, Vol.51 (1), p.120-125</ispartof><rights>2006 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c382t-1492153ab8cdd1189c76fa9ce68884f04419ff84f4cef09bcb2d31caf65f21313</citedby><cites>FETCH-LOGICAL-c382t-1492153ab8cdd1189c76fa9ce68884f04419ff84f4cef09bcb2d31caf65f21313</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S104659280600252X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,4010,27900,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17005417$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fang Hao, Hui</creatorcontrib><creatorcontrib>Li, Xin-Sheng</creatorcontrib><creatorcontrib>Gao, Feng-Shan</creatorcontrib><creatorcontrib>Xue Wu, Wen</creatorcontrib><creatorcontrib>Xia, Chun</creatorcontrib><title>Secondary structure and 3D homology modeling of grass carp ( Ctenopharyngodon idellus) major histocompatibility complex class I molecules</title><title>Protein expression and purification</title><addtitle>Protein Expr Purif</addtitle><description>No information to date is available on the structure of fish major histocompatibility complex (MHC) class I and β2-microglobulin (β2m) proteins. In the present study, grass carp (
Ctenopharyngodon idellus) MHC class I (
Ctid-MHC I) and β
2-microglobulin (
Ctid-β2m) genes were expressed as soluble maltose binding protein (MBP)-proteins and purified in a pMAL-p2X/
Escherichia coli TB1 system. The expressed proteins were purified on amylase affinity columns followed by DEAE–Sepharose. The purified products were identified by Western blotting with anti-MBP polyclonal antibodies. The MBP-
Ctid-MHC I and MBP-
Ctid-β2m were cleaved separately with Factor Xa, mixed together and purified on DEAE–Sepharose. The secondary structures were analyzed by circular dichroism (CD) spectrophotometry. The three-dimensional (3D) structure of their peptide-binding domain (PBD) was modeled based sequence homology. The sequence lengths of the α-helix, β-sheet, turn, and random coil in the
Ctid-MHC I protein were 79
aa, 75
aa, 20
aa, and 99
aa, respectively. In the 97
aa of
Ctid-β2m, the contents of the α-helix, β-sheet, turn, and random coil were 0
aa, 41
aa, 12
aa, and 44
aa, respectively. The
Ctid-β2m protein displayed a typical β-sheet. Homology modeling of the
Ctid-MHC I and
Ctid-β2m proteins demonstrated similarities with the structure of human MHC class I proteins.</description><subject>Animals</subject><subject>beta 2-Microglobulin - chemistry</subject><subject>beta 2-Microglobulin - isolation & purification</subject><subject>Carps - immunology</subject><subject>Circular Dichroism</subject><subject>Circular dichroism spectrum</subject><subject>Ctenopharyngodon idella</subject><subject>Escherichia coli</subject><subject>Genetic Vectors</subject><subject>Grass carp</subject><subject>Histocompatibility Antigens Class I - chemistry</subject><subject>Histocompatibility Antigens Class I - isolation & purification</subject><subject>Homology modeling</subject><subject>MHC I</subject><subject>Models, Molecular</subject><subject>Protein Structure, Secondary</subject><subject>Recombinant Fusion Proteins - biosynthesis</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Secondary structure</subject><subject>β 2-microglobulin</subject><issn>1046-5928</issn><issn>1096-0279</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU2r1DAUhoso3g_9AW4kK9FFa07TpgmuZPTqhQsu1HVIk5OZDG1Tk1acn-C_NmUG3OkqJ_C8D4fzFsULoBVQ4G-P1YxzVVPKKyoqStmj4hqo5CWtO_l4mxtetrIWV8VNSkdKAThtnxZX0FHaNtBdF7-_ogmT1fFE0hJXs6wRiZ4sYR_IIYxhCPsTGYPFwU97EhzZR50SMTrO5DXZLTiF-ZDT0z7YMBGfwWFNb8iojyGSg09LMGGc9eJ7P_jlRLbfgL-IGTbPfXYPaNYB07PiidNDwueX97b4fvfx2-5z-fDl0_3u_UNpmKiXEhpZQ8t0L4y1AEKajjstDXIhRONo04B0Lk-NQUdlb_raMjDa8dbVwIDdFq_O3jmGHyumRY0-mby2njCsSXHBOGcd-y8IspMtEzKDcAZNDClFdGqOfsxHUUDVVpQ6qlyU2opSVKhcVM68vMjXfkT7N3FpJgPvzgDmW_z0GFUyHieD1kc0i7LB_0P_Bwcupl4</recordid><startdate>2007</startdate><enddate>2007</enddate><creator>Fang Hao, Hui</creator><creator>Li, Xin-Sheng</creator><creator>Gao, Feng-Shan</creator><creator>Xue Wu, Wen</creator><creator>Xia, Chun</creator><general>Elsevier Inc</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>7QL</scope><scope>7QO</scope><scope>7T5</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>2007</creationdate><title>Secondary structure and 3D homology modeling of grass carp ( Ctenopharyngodon idellus) major histocompatibility complex class I molecules</title><author>Fang Hao, Hui ; Li, Xin-Sheng ; Gao, Feng-Shan ; Xue Wu, Wen ; Xia, Chun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c382t-1492153ab8cdd1189c76fa9ce68884f04419ff84f4cef09bcb2d31caf65f21313</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Animals</topic><topic>beta 2-Microglobulin - chemistry</topic><topic>beta 2-Microglobulin - isolation & purification</topic><topic>Carps - immunology</topic><topic>Circular Dichroism</topic><topic>Circular dichroism spectrum</topic><topic>Ctenopharyngodon idella</topic><topic>Escherichia coli</topic><topic>Genetic Vectors</topic><topic>Grass carp</topic><topic>Histocompatibility Antigens Class I - chemistry</topic><topic>Histocompatibility Antigens Class I - isolation & purification</topic><topic>Homology modeling</topic><topic>MHC I</topic><topic>Models, Molecular</topic><topic>Protein Structure, Secondary</topic><topic>Recombinant Fusion Proteins - biosynthesis</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Secondary structure</topic><topic>β 2-microglobulin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fang Hao, Hui</creatorcontrib><creatorcontrib>Li, Xin-Sheng</creatorcontrib><creatorcontrib>Gao, Feng-Shan</creatorcontrib><creatorcontrib>Xue Wu, Wen</creatorcontrib><creatorcontrib>Xia, Chun</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Immunology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Protein expression and purification</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fang Hao, Hui</au><au>Li, Xin-Sheng</au><au>Gao, Feng-Shan</au><au>Xue Wu, Wen</au><au>Xia, Chun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Secondary structure and 3D homology modeling of grass carp ( Ctenopharyngodon idellus) major histocompatibility complex class I molecules</atitle><jtitle>Protein expression and purification</jtitle><addtitle>Protein Expr Purif</addtitle><date>2007</date><risdate>2007</risdate><volume>51</volume><issue>1</issue><spage>120</spage><epage>125</epage><pages>120-125</pages><issn>1046-5928</issn><eissn>1096-0279</eissn><abstract>No information to date is available on the structure of fish major histocompatibility complex (MHC) class I and β2-microglobulin (β2m) proteins. In the present study, grass carp (
Ctenopharyngodon idellus) MHC class I (
Ctid-MHC I) and β
2-microglobulin (
Ctid-β2m) genes were expressed as soluble maltose binding protein (MBP)-proteins and purified in a pMAL-p2X/
Escherichia coli TB1 system. The expressed proteins were purified on amylase affinity columns followed by DEAE–Sepharose. The purified products were identified by Western blotting with anti-MBP polyclonal antibodies. The MBP-
Ctid-MHC I and MBP-
Ctid-β2m were cleaved separately with Factor Xa, mixed together and purified on DEAE–Sepharose. The secondary structures were analyzed by circular dichroism (CD) spectrophotometry. The three-dimensional (3D) structure of their peptide-binding domain (PBD) was modeled based sequence homology. The sequence lengths of the α-helix, β-sheet, turn, and random coil in the
Ctid-MHC I protein were 79
aa, 75
aa, 20
aa, and 99
aa, respectively. In the 97
aa of
Ctid-β2m, the contents of the α-helix, β-sheet, turn, and random coil were 0
aa, 41
aa, 12
aa, and 44
aa, respectively. The
Ctid-β2m protein displayed a typical β-sheet. Homology modeling of the
Ctid-MHC I and
Ctid-β2m proteins demonstrated similarities with the structure of human MHC class I proteins.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17005417</pmid><doi>10.1016/j.pep.2006.08.003</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Protein expression and purification, 2007, Vol.51 (1), p.120-125 |
| issn | 1046-5928 1096-0279 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_68366373 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals beta 2-Microglobulin - chemistry beta 2-Microglobulin - isolation & purification Carps - immunology Circular Dichroism Circular dichroism spectrum Ctenopharyngodon idella Escherichia coli Genetic Vectors Grass carp Histocompatibility Antigens Class I - chemistry Histocompatibility Antigens Class I - isolation & purification Homology modeling MHC I Models, Molecular Protein Structure, Secondary Recombinant Fusion Proteins - biosynthesis Recombinant Fusion Proteins - chemistry Secondary structure β 2-microglobulin |
| title | Secondary structure and 3D homology modeling of grass carp ( Ctenopharyngodon idellus) major histocompatibility complex class I molecules |
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