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)