The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
HLA-A2-peptide complexes: refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides.
Open accessAbstract
The two subunits of the human class I histocompatibility antigen (HLA)-A2 have been expressed at high levels (20-30 mg/liter) as insoluble aggregates in bacterial cells. The aggregates were dissolved in 8 M urea and then refolded to form an HLA-A2-peptide complex by removal of urea in the presence of an antigenic peptide. Two peptides from the matrix protein and nucleoprotein of influenza virus are known to bind to HLA-A2, and both support the refolding of the recombinant HLA-A2 molecule. An additional peptide, a nonamer from the gp120 envelope protein of human immunodeficiency virus type 1, also supported refolding. Yields of purified recombinant HLA-A2 are 10-15%. In the absence of an HLA-A2-restricted peptide, a stable HLA-A2 complex was not formed. Monoclonal antibodies known to bind to native HLA-A2 also bound to the recombinant HLA-A2-peptide complex. Three purified HLA-A2-peptide complexes refolded from bacterially produced protein aggregates crystallize under the identical conditions as HLA-A2 purified from human lymphoblastoid cells. Crystals of the recombinant HLA-A2 molecule in complex with the influenza matrix nonamer peptide, Mp(58-66), diffract to greater than 1.5-A resolution.
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Metadata
- Authors
- Garboczi, D. N., Hung, D. T., & Wiley, D. C.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1992-04-15
- Volume
- 89
- Issue
- 8
- Pages
- 3429-3433
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1995138538
- Cited by
- 689
- References
- 1
- FWCI
- 2.29
- Type
- journal article
- Language
- en
- Open access
- green
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- Garboczi, D. N., Hung, D. T., & Wiley, D. C. (1992). HLA-A2-peptide complexes: refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.89.8.3429
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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