Refolding and reassembly of separate alpha and beta chains of class II molecules of the major histocompatibility complex leads to increased peptide-binding capacity.
AUTOR(ES)
Dornmair, K
RESUMO
Class II molecules of the major histocompatibility complex present antigenic peptides to helper T cells. These are heterodimeric glycoproteins consisting of one alpha and one beta chain. Two different alpha/beta heterodimeric conformations as well as the separate alpha and beta chains bind specific peptides. The alpha chain is thought to have one and the beta chain two intramolecular disulfide bonds. In the present study we have reduced these disulfide bonds in the murine major histocompatibility complex molecule I-Ad, which led to the release of bound peptides from all conformations and to unfolding of the separate chains. The separate alpha and beta chains could be refolded to their native structure by reoxidation of the cysteines. Refolding was accompanied by reassembly of the separated chains to the alpha/beta heterodimer. Both the separated alpha and beta chains and the alpha/beta heterodimer bound significantly higher amounts of antigenic peptide after reduction and reoxidation, as compared to the untreated protein.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=54062Documentos Relacionados
- Specific binding of antigenic peptides to separate alpha and beta chains of class II molecules of the major histocompatibility complex.
- Effects of pH and polysaccharides on peptide binding to class II major histocompatibility complex molecules.
- Binding of an invariant-chain peptide, CLIP, to I-A major histocompatibility complex class II molecules.
- Molecular Determinants of Peptide Binding to Two Common Rhesus Macaque Major Histocompatibility Complex Class II Molecules
- Stimulation of T cells by antigenic peptide complexed with isolated chains of major histocompatibility complex class II molecules.