Amino Acid Residues Essential for Biological Activity of a Peptide Derived From a Major Histocompatibility Complex Class I Antigen Amino Acid Residues Essential for Biological Activity of a Peptide Derived From a Major Histocompatibility Complex Class I Antigen

Contributor(s): Matthews, Brian W. Meyers, Chester Mapelli, Claudio Anfinsen, Christian B. (Christian Boehmer), 1916-1995 Olsson, Lennart Goldstein, Avram Stagsted, Jan Proceedings of the National Academy of Sciences of the United States of America Publication: National Academy Press (U.S.), 1993 Language(s): English Format: Text Subject(s): Amino Acid Sequence Protein Conformation Histocompatibility Peptides Genre(s): Archival Materials Articles Abstract: 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. Copyright: This item may be under copyright protection; contact the copyright owner for permission before re-use. Extent: 5 pages NLM Unique ID: 101584571X159 (See in Profiles in Science) Profiles in Science ID: KKBBKQ Permanent Link: http://resource.nlm.nih.gov/101584571X159 Archival Collection: The Christian B. Anfinsen Papers (Profiles in Science)