(PDF) A Mutational Analysis of the Binding of

A Mutational Analysis of the Binding of Staphylococcal Enterotoxins B and C3 to the T Cell Receptor Β Chain and Major Histocompatibility Complex Class II

Journal of Experimental Medicine - United States

doi 10.1084/jem.187.6.823

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Date

March 16, 1998

Authors

Patrick M. Schlievert

Klaus Karjalainen

Roy A. Mariuzza

Publisher

Rockefeller University Press

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A Mutational Analysis of the Binding of Staphylococcal Enterotoxins B and C3 to the T Cell Receptor Β Chain and Major Histocompatibility Complex Class II

Journal of Experimental Medicine - United States

doi 10.1084/jem.187.6.823

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Specific T Cell Recognition of Kinetic Isomers in the Binding of Peptide to Class II Major Histocompatibility Complex

The Contribution of Major Histocompatibility Complex Contacts to the Affinity and Kinetics of T Cell Receptor Binding

Ii Chain Controls the Transport of Major Histocompatibility Complex Class II Molecules to and From Lysosomes

Differential Immune Responses to Staphylococcal Enterotoxin B Mutations in a Hydrophobic Loop Dominating the Interface With Major Histocompatibility Complex Class II Receptors

CD8+ T Cell Response to MLS-1a Determinants Involves Major Histocompatibility Complex Class II Molecules

Major Histocompatibility Complex Class I Diversity Limits the Repertoire of T Cell Receptors

A First-Order Reaction Controls the Binding of Antigenic Peptides to Major Histocompatibility Complex Class II Molecules.

Invariant Chain Cleavage and Peptide Loading in Major Histocompatibility Complex Class II Vesicles

Function of NF-kappa B/Rel Binding Sites in the Major Histocompatibility Complex Class II Invariant Chain Promoter Is Dependent on Cell-Specific Binding of Different NF-kappa B/Rel Subunits.