Glu227-->Lys substitution in the acidic loop of major histocompatibility complex class I alpha 3 domain distinguishes low avidity CD8 coreceptor and avidity-enhanced CD8 accessory functions.

doi:10.1084/jem.184.5.1671

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Article

Glu227-->Lys substitution in the acidic loop of major histocompatibility complex class I alpha 3 domain distinguishes low avidity CD8 coreceptor and avidity-enhanced CD8 accessory functions.

The Journal of experimental medicine - 1 Nov 1996

Shen L, Potter T A, Kane K P

Abstract excerpt

Cytotoxic T lymphocyte (CTL) activation requires specific T cell receptor (TCR)-class I major histocompatibility complex (MHC) antigen complex interactions as well as the participation of coreceptor or accessory molecules on the surface of CTL. CD8 can serve as a coreceptor in that it binds to th...

Topics

Binding Sites
CD8 Antigens
Cell Adhesion
Cell Degranulation
Clone Cells
Cytotoxicity, Immunologic
Glutamic Acid
H-2 Antigens
Histocompatibility Antigens Class I
Ligands
Lymphocyte Activation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Lysine

Mutation

Peptide Fragments

Protein Conformation

Receptors, Antigen, T-Cell

Recombinant Fusion Proteins

Signal Transduction

Source

Open in PubMed Open full text

Identifiers

PMID: 8920857
DOI: 10.1084/jem.184.5.1671
PMCID: PMC2192880

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8920857-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Glu227-->Lys substitution in the acidic loop of major histocompatibility complex class I alpha 3 domain distinguishes low avidity CD8 coreceptor and avidity-enhanced CD8 accessory functions.PMID 8920857Read ↗

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