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- W2053647970 abstract "The tremendous explosion in the field of MHC research in the last 5 years has significantly advanced our understanding of antigen processing pathways, particularly with regard to details of MHC class II‐mediated antigen presentation. MHC class II molecules at the surface of antigen presenting cells present antigenie peptides to CD4 + T helper cells. However for effective cell surface antigen presentation, a number of highly synchronized events must first take place intracellularly. The monomorphic protein, invariant chain (Ii), is a crucial participant in MHC class II antigen presentation. Acting as a molecular chaperone, this molecule escorts the newly synthesized class II heterodimers from the endoplasmic reticulum into the endosomal system. During this manoeuvre, the interaction of Ii with class II serves to prevent premature association of antigenic peptide. Once the complex reaches the acidic environment of the endosomes, Ii is proteolytically degraded and dissociates, leaving the class II binding site available for binding antigenic peptide derived from exogenous proteins. The final Ii fragment to be displaced. CLIP (class II‐associated invariant chain peptides), must be physically removed from the class II binding groove with assistance from another MHC‐encoded molecule. DM. The interaction of DM with class II also aids in the subsequent rapid loading of high‐affinity antigen‐derived peptides into the MHC class II groove. The stable peptide‐loaded complexes are now ready to exit the endocytic compartments to present their peptide antigen to specific T helper cells at the cell surface." @default.
- W2053647970 created "2016-06-24" @default.
- W2053647970 creator A5001514335 @default.
- W2053647970 creator A5063238507 @default.
- W2053647970 date "1997-02-01" @default.
- W2053647970 modified "2023-09-30" @default.
- W2053647970 title "Antigen presentation by MHC class II molecules" @default.
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