Amino Acid Residues Essential for Biological Activity of a Peptide Derived From a Major Histocompatibility Complex Class I
In this article, Anfinsen, in collaboration with a number of scientists at laboratories across the United States, reported
his observations on the self interaction of peptides from the alpha-1 domain of the major histocampatibility complex (MHC)
class I antigen. The authors noted that this self interaction, in the absence of cells and form aggregates that precipitate
upon centrifugation, suggested that the biological effects in cells, which result from inhibition of receptor and transporter
internalization, may be due to the binding of the peptide to the homologous sequences in the alpha-1 domain of the MHC class
I molecule. The researchers suggested that MHC class I molecules, which function in the immune system to transport antigenic
peptides to the cell surface, might also play a role in receptor recycling.
Number of Image Pages:
5 (691,995 Bytes)
Matthews, Brian W.
Anfinsen, Christian B.
Periodical: Stagsted, Jan, Claudio Mapelli, Chester Meyers, Brian W. Matthews, Christian B. Anfinsen, Avram Goldstein, and Lennart Olsson.
"Amino Acid Residues Essential for Biological Activity of a Peptide Derived From a Major Histocompatibility Complex Class
I Antigen." Proceedings of the National Academy of Sciences of the United States of America 90, (1993): 7686-7690. Article.
National Academy Press
Reproduced with permission of the National Academy of Sciences (U.S.).