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

 Digital Record
Identifier: 101584571X159

Dates

  • Publication: 1993

Extent

5 Pages

Description

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.

Language of Materials

English

Original Profiles System Identifier

KKBBKQ

Source Category

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. 5 Images.

Proceedings of the National Academy of Sciences of the United States of America

Physical Description

Physical Condition - Good

Collecting Area Details

Part of the Archives and Modern Manuscripts Collection Collecting Area

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