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Muteins of human interleukin‐1 that show enhanced bioactivities
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| Zeitschriftentitel: | FEBS Letters |
|---|---|
| Personen und Körperschaften: | , , , , , , |
| In: | FEBS Letters, 223, 1987, 2, S. 294-298 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Huang, James J. Newton, Robert C. Horuk, Richard Matthew, James B. Covington, Maryanne Pezzella, Kathleen Lin, Yuan Huang, James J. Newton, Robert C. Horuk, Richard Matthew, James B. Covington, Maryanne Pezzella, Kathleen Lin, Yuan |
|---|---|
| author |
Huang, James J. Newton, Robert C. Horuk, Richard Matthew, James B. Covington, Maryanne Pezzella, Kathleen Lin, Yuan |
| spellingShingle |
Huang, James J. Newton, Robert C. Horuk, Richard Matthew, James B. Covington, Maryanne Pezzella, Kathleen Lin, Yuan FEBS Letters Muteins of human interleukin‐1 that show enhanced bioactivities Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| author_sort |
huang, james j. |
| spelling |
Huang, James J. Newton, Robert C. Horuk, Richard Matthew, James B. Covington, Maryanne Pezzella, Kathleen Lin, Yuan 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/0014-5793(87)80307-1 <jats:p>Using recombinant DNA techniques, we have made a series of amino‐terminal muteins of human interleukin‐1 (IL‐1). Two of the muteins demonstrated 4–7‐fold increase in bioactivity as compared to that of the native IL‐1. The enhanced biological potency coincides with an increase in both receptor binding affinity and in vivo tumor inhibitory activity. By site specific mutagenesis, we have shown that the arginine at the fourth position of IL‐1 is one of the key residues in the function of IL‐1. Circular dichroism studies of the amino‐terminus analogs showed little structural rearrangement. The change in bioactivity might be due to a change in the stability of the muteins, in the side chain interactions with receptors or in the minor change in folding near the receptor binding site.</jats:p> Muteins of human interleukin‐1 that show enhanced bioactivities FEBS Letters |
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10.1016/0014-5793(87)80307-1 |
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| imprint |
Wiley, 1987 |
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Wiley, 1987 |
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1873-3468 0014-5793 |
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1873-3468 0014-5793 |
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1987 |
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Wiley |
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FEBS Letters |
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| title |
Muteins of human interleukin‐1 that show enhanced bioactivities |
| title_unstemmed |
Muteins of human interleukin‐1 that show enhanced bioactivities |
| title_full |
Muteins of human interleukin‐1 that show enhanced bioactivities |
| title_fullStr |
Muteins of human interleukin‐1 that show enhanced bioactivities |
| title_full_unstemmed |
Muteins of human interleukin‐1 that show enhanced bioactivities |
| title_short |
Muteins of human interleukin‐1 that show enhanced bioactivities |
| title_sort |
muteins of human interleukin‐1 that show enhanced bioactivities |
| topic |
Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| url |
http://dx.doi.org/10.1016/0014-5793(87)80307-1 |
| publishDate |
1987 |
| physical |
294-298 |
| description |
<jats:p>Using recombinant DNA techniques, we have made a series of amino‐terminal muteins of human interleukin‐1 (IL‐1). Two of the muteins demonstrated 4–7‐fold increase in bioactivity as compared to that of the native IL‐1. The enhanced biological potency coincides with an increase in both receptor binding affinity and in vivo tumor inhibitory activity. By site specific mutagenesis, we have shown that the arginine at the fourth position of IL‐1 is one of the key residues in the function of IL‐1. Circular dichroism studies of the amino‐terminus analogs showed little structural rearrangement. The change in bioactivity might be due to a change in the stability of the muteins, in the side chain interactions with receptors or in the minor change in folding near the receptor binding site.</jats:p> |
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| author | Huang, James J., Newton, Robert C., Horuk, Richard, Matthew, James B., Covington, Maryanne, Pezzella, Kathleen, Lin, Yuan |
| author_facet | Huang, James J., Newton, Robert C., Horuk, Richard, Matthew, James B., Covington, Maryanne, Pezzella, Kathleen, Lin, Yuan, Huang, James J., Newton, Robert C., Horuk, Richard, Matthew, James B., Covington, Maryanne, Pezzella, Kathleen, Lin, Yuan |
| author_sort | huang, james j. |
| container_issue | 2 |
| container_start_page | 294 |
| container_title | FEBS Letters |
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| description | <jats:p>Using recombinant DNA techniques, we have made a series of amino‐terminal muteins of human interleukin‐1 (IL‐1). Two of the muteins demonstrated 4–7‐fold increase in bioactivity as compared to that of the native IL‐1. The enhanced biological potency coincides with an increase in both receptor binding affinity and in vivo tumor inhibitory activity. By site specific mutagenesis, we have shown that the arginine at the fourth position of IL‐1 is one of the key residues in the function of IL‐1. Circular dichroism studies of the amino‐terminus analogs showed little structural rearrangement. The change in bioactivity might be due to a change in the stability of the muteins, in the side chain interactions with receptors or in the minor change in folding near the receptor binding site.</jats:p> |
| doi_str_mv | 10.1016/0014-5793(87)80307-1 |
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| finc_class_facet | Biologie, Chemie und Pharmazie, Physik |
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| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTAxNi8wMDE0LTU3OTMoODcpODAzMDctMQ |
| imprint | Wiley, 1987 |
| imprint_str_mv | Wiley, 1987 |
| institution | DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1 |
| issn | 1873-3468, 0014-5793 |
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| language | English |
| last_indexed | 2024-03-01T15:12:47.907Z |
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| mega_collection | Wiley (CrossRef) |
| physical | 294-298 |
| publishDate | 1987 |
| publishDateSort | 1987 |
| publisher | Wiley |
| record_format | ai |
| recordtype | ai |
| series | FEBS Letters |
| source_id | 49 |
| spelling | Huang, James J. Newton, Robert C. Horuk, Richard Matthew, James B. Covington, Maryanne Pezzella, Kathleen Lin, Yuan 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/0014-5793(87)80307-1 <jats:p>Using recombinant DNA techniques, we have made a series of amino‐terminal muteins of human interleukin‐1 (IL‐1). Two of the muteins demonstrated 4–7‐fold increase in bioactivity as compared to that of the native IL‐1. The enhanced biological potency coincides with an increase in both receptor binding affinity and in vivo tumor inhibitory activity. By site specific mutagenesis, we have shown that the arginine at the fourth position of IL‐1 is one of the key residues in the function of IL‐1. Circular dichroism studies of the amino‐terminus analogs showed little structural rearrangement. The change in bioactivity might be due to a change in the stability of the muteins, in the side chain interactions with receptors or in the minor change in folding near the receptor binding site.</jats:p> Muteins of human interleukin‐1 that show enhanced bioactivities FEBS Letters |
| spellingShingle | Huang, James J., Newton, Robert C., Horuk, Richard, Matthew, James B., Covington, Maryanne, Pezzella, Kathleen, Lin, Yuan, FEBS Letters, Muteins of human interleukin‐1 that show enhanced bioactivities, Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| title | Muteins of human interleukin‐1 that show enhanced bioactivities |
| title_full | Muteins of human interleukin‐1 that show enhanced bioactivities |
| title_fullStr | Muteins of human interleukin‐1 that show enhanced bioactivities |
| title_full_unstemmed | Muteins of human interleukin‐1 that show enhanced bioactivities |
| title_short | Muteins of human interleukin‐1 that show enhanced bioactivities |
| title_sort | muteins of human interleukin‐1 that show enhanced bioactivities |
| title_unstemmed | Muteins of human interleukin‐1 that show enhanced bioactivities |
| topic | Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| url | http://dx.doi.org/10.1016/0014-5793(87)80307-1 |