The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Site-Specific Mutagenesis of the Human Interleukin-2 Gene: Structure-Function Analysis of the Cysteine Residues
Abstract
The gene encoding human interleukin-2 (IL-2) has been cloned from human spleen cells, peripheral blood lymphocytes, and the Jurkat cell line. Nucleotide sequence analysis of the gene revealed that the encoded IL-2 protein has three cysteines located at amino acid residues 58, 105, and 125 of the mature protein. Site-specific mutagenesis procedures were used to modify the IL-2 gene by changing each of the cysteine codons individually to serine codons. Substitution of serine for cysteine residues at either position 58 or 105 of the IL-2 protein substantially reduced biological activity, indicating that the cysteines at these positions are necessary for maintenance of the biologically active conformation and may therefore be linked by a disulfide bridge. The modified IL-2 protein containing a substitution at position 125 retained full biological activity, suggesting that the cysteine at this position is not involved in a disulfide bond and that a free sulfhydryl group at that position is not necessary for receptor binding.
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Cited by
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Factors affecting short-term and long-term stabilities of proteins
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Molecular Cloning of the Complementary DNA for Human Tumor Necrosis Factor
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Metadata
- Authors
- Wang, A., Lu, S.-D., & Mark, D. F.
- Venue
- Science
- Published
- 1984-06-29
- Volume
- 224
- Issue
- 4656
- Pages
- 1431-1433
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2090741624
- Cited by
- 324
- References
- 17
- FWCI
- 15.69
- Type
- journal article
- Language
- en
- Open access
- closed
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- Wang, A., Lu, S.-D., & Mark, D. F. (1984). Site-Specific Mutagenesis of the Human Interleukin-2 Gene: Structure-Function Analysis of the Cysteine Residues. Science. https://doi.org/10.1126/science.6427925
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