Computer-aided modeling of structure stabilizing disulfide bonds in recombinant human interferon-γ
We present a general search algorithm for possible insertion sites of disulfide bonds in proteins based on the coordinates of the solved X-ray or NMR structure, allowing the insertion of disulfide bonds with a minimum of conformational tension and backbone rearrangements. The fortran 77 program ‘Ssu...
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| Published in | Pharmaceutica acta Helvetiae Vol. 71; no. 1; pp. 37 - 44 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Switzerland
Elsevier B.V
01.06.1996
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| Subjects | |
| Online Access | Get full text |
| ISSN | 0031-6865 |
| DOI | 10.1016/0031-6865(95)00045-3 |
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| Abstract | We present a general search algorithm for possible insertion sites of disulfide bonds in proteins based on the coordinates of the solved X-ray or NMR structure, allowing the insertion of disulfide bonds with a minimum of conformational tension and backbone rearrangements. The fortran 77 program ‘Ssuitable’ was written for this purpose. This methodological approach was applied to recombinant human interferon-γ (rhu-IFN-γ), a cytokine of great pharmaceutical interest with a wide variety of biological activities including antiviral, antiproliferative and immunomodulatory effects. A model based on the CMα-coordinates obtained from the Brookhaven data base was built. Four different insertion sites were selected in the model, connecting the two subunits of the homodimer. The thermodynamic stability of rhu-IFN-γ is low, limiting its clinical application. We expect that the insertion of additional new disulfide bonds will enhance the thermodynamic stability as well as protect the protein against proteolytic degradation. |
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| AbstractList | We present a general search algorithm for possible insertion sites of disulfide bonds in proteins based on the coordinates of the solved X-ray or NMR structure, allowing the insertion of disulfide bonds with a minimum of conformational tension and backbone rearrangements. The FORTRAN 77 program "Ssuitable' was written for this purpose. This methodological approach was applied to recombinant human interferon-gamma (rhu-IFN-gamma), a cytokine of great pharmaceutical interest with a wide variety of biological activities including antiviral, antiproliferative and immunomodulatory effects. A model based on the C alpha-coordinates obtained from the Brookhaven data base was built. Four different insertion sites were selected in the model, connecting the two subunits of the homodimer. The thermodynamic stability of rhu-IFN-gamma is low, limiting its clinical application. We expect that the insertion of additional new disulfide bonds will enhance the thermodynamic stability as well as protect the protein against proteolytic degradation.We present a general search algorithm for possible insertion sites of disulfide bonds in proteins based on the coordinates of the solved X-ray or NMR structure, allowing the insertion of disulfide bonds with a minimum of conformational tension and backbone rearrangements. The FORTRAN 77 program "Ssuitable' was written for this purpose. This methodological approach was applied to recombinant human interferon-gamma (rhu-IFN-gamma), a cytokine of great pharmaceutical interest with a wide variety of biological activities including antiviral, antiproliferative and immunomodulatory effects. A model based on the C alpha-coordinates obtained from the Brookhaven data base was built. Four different insertion sites were selected in the model, connecting the two subunits of the homodimer. The thermodynamic stability of rhu-IFN-gamma is low, limiting its clinical application. We expect that the insertion of additional new disulfide bonds will enhance the thermodynamic stability as well as protect the protein against proteolytic degradation. We present a general search algorithm for possible insertion sites of disulfide bonds in proteins based on the coordinates of the solved X-ray or NMR structure, allowing the insertion of disulfide bonds with a minimum of conformational tension and backbone rearrangements. The fortran 77 program ‘Ssuitable’ was written for this purpose. This methodological approach was applied to recombinant human interferon-γ (rhu-IFN-γ), a cytokine of great pharmaceutical interest with a wide variety of biological activities including antiviral, antiproliferative and immunomodulatory effects. A model based on the CMα-coordinates obtained from the Brookhaven data base was built. Four different insertion sites were selected in the model, connecting the two subunits of the homodimer. The thermodynamic stability of rhu-IFN-γ is low, limiting its clinical application. We expect that the insertion of additional new disulfide bonds will enhance the thermodynamic stability as well as protect the protein against proteolytic degradation. We present a general search algorithm for possible insertion sites of disulfide bonds in proteins based on the coordinates of the solved X-ray or NMR structure, allowing the insertion of disulfide bonds with a minimum of conformational tension and backbone rearrangements. The FORTRAN 77 program "Ssuitable' was written for this purpose. This methodological approach was applied to recombinant human interferon-gamma (rhu-IFN-gamma), a cytokine of great pharmaceutical interest with a wide variety of biological activities including antiviral, antiproliferative and immunomodulatory effects. A model based on the C alpha-coordinates obtained from the Brookhaven data base was built. Four different insertion sites were selected in the model, connecting the two subunits of the homodimer. The thermodynamic stability of rhu-IFN-gamma is low, limiting its clinical application. We expect that the insertion of additional new disulfide bonds will enhance the thermodynamic stability as well as protect the protein against proteolytic degradation. |
| Author | Fechteler, Till Villmann, Carmen Schomburg, Dietmar Zakaria, Hayssam Günther, Gero Otto, Bernd |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/8786998$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1021/bi00382a017 10.1016/S0021-9258(18)66737-7 10.1021/bi00368a023 10.1021/bi00368a024 10.1038/363172a0 10.1093/protein/5.3.253 10.1126/science.6387910 10.1093/protein/2.2.119 10.1021/bi00465a026 10.1093/protein/4.3.335 10.1021/bi00437a043 10.1016/0263-7855(88)80069-9 10.1016/S0021-9258(19)84599-4 10.1016/0022-2836(81)90515-5 10.1021/bi00133a008 10.1093/protein/3.2.95 10.1016/S0021-9258(18)63838-4 10.1111/j.1432-1033.1991.tb16481.x 10.1016/S0022-2836(05)80018-X 10.1126/science.1902591 10.1089/jir.1992.12.139 |
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| Keywords | Interferon Computer modeling Disulfide bridges |
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Biol. doi: 10.1016/S0022-2836(05)80018-X – volume: 8 start-page: 57 year: 1988 ident: 10.1016/0031-6865(95)00045-3_BIB4 article-title: Disulfide bonds and protein stability publication-title: Bio Essays – volume: 252 start-page: 698 year: 1991 ident: 10.1016/0031-6865(95)00045-3_BIB6 article-title: Three-dimensional structure of recombinant human Interferon-γ publication-title: Science doi: 10.1126/science.1902591 – volume: 90 start-page: 7538 year: 1993 ident: 10.1016/0031-6865(95)00045-3_BIB3 article-title: A recombinant immunotoxin containing a disulfide-stabilized Fv fragment – volume: 12 start-page: 139 year: 1992 ident: 10.1016/0031-6865(95)00045-3_BIB5 article-title: Engineered disulfide bond greatly increases specific activity of recombinant murine interferon-β publication-title: J. Interferon Res. doi: 10.1089/jir.1992.12.139 |
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| SubjectTerms | Amino Acid Sequence Computer modeling Computer Simulation Disulfide bridges Disulfides - chemistry Humans Interferon Interferon-gamma - chemistry Models, Structural Molecular Sequence Data Recombinant Proteins |
| Title | Computer-aided modeling of structure stabilizing disulfide bonds in recombinant human interferon-γ |
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