ArticleProtein science : a publication of the Protein Society1998
Assembly and crystallization of the complex between the human T cell coreceptor CD8alpha homodimer and HLA-A2.
Article in Protein science : a publication of the Protein Society, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 24 citations in OpenAlex.
- Reconciling views on T cell receptor germline bias for MHC.Trends in immunology · 2012Article
- Crystallization and preliminary X-ray crystallographic studies of swine CD8α.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Expression, purification, crystallization and preliminary X-ray diffraction analysis of rhesus macaque CD8alphaalpha homodimer.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- A dimeric structure of PD-L1: functional units or evolutionary relics?Protein & cell · 2010Article
- Interaction between the CD8 coreceptor and major histocompatibility complex class I stabilizes T cell receptor-antigen complexes at the cell surface.The Journal of biological chemistry · 2005Article
- Refolding, crystallization and preliminary X-ray structural studies of the West Nile virus envelope (E) protein domain III.Acta crystallographica. Section F, Structural biology and crystallization communications · 2005Article
- Crystallization and preliminary X-ray structural studies of a high-affinity CD8alphaalpha co-receptor to pMHC.Acta crystallographica. Section F, Structural biology and crystallization communications · 2005Article
- Human inhibitory receptors Ig-like transcript 2 (ILT2) and ILT4 compete with CD8 for MHC class I binding and bind preferentially to HLA-G.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Structure of a functional IGF2R fragment determined from the anomalous scattering of sulfur.The EMBO journal · 2002Article
- Production of soluble alphabeta T-cell receptor heterodimers suitable for biophysical analysis of ligand binding.Protein science : a publication of the Protein Society · 1999Article
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A strategy for overexpression in Escherichia coli of the extracellular immunoglobulin domain of human CD8alpha was devised using codon usage alterations in the 5' region of the gene, designed so as to prevent the formation of secondary structures in the mRNA. A fragment of CD8alpha, comprising residues 1-120 of the mature protein, excluding the signal peptide and the membrane-proximal stalk region, was recovered from bacterial inclusion bodies and refolded to produce a single species of homodimeric, soluble receptor. HLA-A2 heavy chain, beta2-microglobulin and a synthetic peptide antigen corresponding to the pol epitope from HIV-1 were also expressed in E. coli, refolded and purified. CD8alpha/HLA-A2 complexes were formed in solution and by co-crystallization with a stoichiometry of one CD8alpha alpha dimer to one HLA-A2-peptide unit.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.