Noble metals strip peptides from class II MHC proteins View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2006-04

AUTHORS

Stephen L De Wall, Corrie Painter, Jennifer D Stone, Rajintha Bandaranayake, Don C Wiley, Timothy J Mitchison, Lawrence J Stern, Brian S DeDecker

ABSTRACT

Class II major histocompatibility complex (MHC) proteins are essential for normal immune system function but also drive many autoimmune responses. They bind peptide antigens in endosomes and present them on the cell surface for recognition by CD4(+) T cells. A small molecule could potentially block an autoimmune response by disrupting MHC-peptide interactions, but this has proven difficult because peptides bind tightly and dissociate slowly from MHC proteins. Using a high-throughput screening assay we discovered a class of noble metal complexes that strip peptides from human class II MHC proteins by an allosteric mechanism. Biochemical experiments indicate the metal-bound MHC protein adopts a 'peptide-empty' conformation that resembles the transition state of peptide loading. Furthermore, these metal inhibitors block the ability of antigen-presenting cells to activate T cells. This previously unknown allosteric mechanism may help resolve how gold(I) drugs affect the progress of rheumatoid arthritis and may provide a basis for developing a new class of anti-autoimmune drugs. More... »

PAGES

197

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nchembio773

DOI

http://dx.doi.org/10.1038/nchembio773

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1006821974

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16505807


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