An HLA-A2/β2-microglobulin/peptide complex assembled from subunits expressed separately in Escherichia coli

Parker, Kenneth C.; Silver, Michael L.; Wiley, Don C.

doi:10.1016/0161-5890(92)90024-r

Cited by 12 publications

(1 citation statement)

References 32 publications

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“…The first structures determined for class I and class II histocompatibility proteins (Table 1) were of proteins, purified from their native sources, which retained the collection of peptides bound in vivo and presented at the cell surface. Heterologous expression of histocompatibility proteins in cells which fold them correctly but do not load peptides (Spodoptera [1], Drosophila [2]), and the refolding of histocompatibility proteins from denatured subunits [3][4][5], have led to the availability of complexes of class I and II histocompatibility proteins with single, defined peptides. The three-dimensional structures of several of these complexes have recently been determined by X-ray crystallography (Table 1).…”

Section: Lawrence Stern and Don C Wiley Reviewmentioning

confidence: 99%

Antigenic peptide binding by class I and class II histocompatibility proteins

1994

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Section: Lawrence Stern and Don C Wiley Reviewmentioning

confidence: 99%

Antigenic peptide binding by class I and class II histocompatibility proteins

1994

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The assembly of H2‐K^b class I molecules translated in vitro requires oxidized glutathione and peptide

et al. 1993

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Association of the mouse major histocompatibility complex (MHC) class I heavy chain H2-Kb with mouse beta 2-microglobulin (beta 2m) was studied in an in vitro translation system. Formation of stable class I complexes was found to be dependent on the presence of presentable peptides and oxidized glutathione, which promotes the formation of disulfide bridges. Translocation of peptides into microsomes was demonstrated by showing that a radioiodinated peptide containing an N-glycosylation acceptor site became glycosylated. Class I complex formation was observed only when heavy chains and beta 2m were translated simultaneously, and thus occurs in the microsomes and not after their solubilization. However, peptide binding takes place only after solubilization of the microsomes. The class I complexes translated in vitro show the same specificity and length preference for peptides as their counterparts in RMA-S cells. Assembly of in vitro translated class I complexes was found to occur also in the absence of peptides, resulting in the formation of unstable molecules that are stabilized by incubation with peptides.

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Analysis of MHC-Specific Peptide Motifs

Loftus

Kubo

Sakaguchi

et al. 1995

Advances in Experimental Medicine and Biology

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An HLA-A2/β2-microglobulin/peptide complex assembled from subunits expressed separately in Escherichia coli

Cited by 12 publications

References 32 publications

Antigenic peptide binding by class I and class II histocompatibility proteins

Antigenic peptide binding by class I and class II histocompatibility proteins

The assembly of H2‐K^b class I molecules translated in vitro requires oxidized glutathione and peptide

Analysis of MHC-Specific Peptide Motifs

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An HLA-A2/β2-microglobulin/peptide complex assembled from subunits expressed separately in Escherichia coli

Cited by 12 publications

References 32 publications

Antigenic peptide binding by class I and class II histocompatibility proteins

Antigenic peptide binding by class I and class II histocompatibility proteins

The assembly of H2‐Kb class I molecules translated in vitro requires oxidized glutathione and peptide

Analysis of MHC-Specific Peptide Motifs

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The assembly of H2‐K^b class I molecules translated in vitro requires oxidized glutathione and peptide