Related Experiment Video
Updated: Jul 14, 2026

Measuring TCR-pMHC Binding In Situ using a FRET-based Microscopy Assay
Published on: October 30, 2015
Degenerate binding of tyrosinase peptides to MHC II Ad/Ed molecules
Abraham Mittelman1, Guglielmo Lucchese, Angela Stufano
1Department of Medicine/Oncology, New York Medical College, Valhalla, NY 10595, USA.
Abstract:
Recently we defined the tyrosinase233-247IPYWDWRDAEKCDIC peptide as the pentadecamer sequence hosting the linear determinant of the anti-tyrosinase MAb T311. In order to understand the molecular features that render epitopic the amino acid tyrosinase233-247 sequence, we 1) analyzed the MHC II affinity of the tyrosinase233-247IPYWDWRDAEKCDIC peptide using RankPep as a binding prediction program, and 2) experimentally verified the actual peptide-MHC II interaction by carrying out peptide electrophoretic mobility shift assays. Nine random tyrosinase peptides were used as controls. Under the conditions used in this study, it was found that all of the ten tyrosinase peptides were capable of binding to Ad/Ed molecules in the gel-shift binding assay. Moreover, there was no correlation between the theoretical predicted Ad/Ed affinity and the experimental actual peptide binding. We conclude that Ad/Ed binding potential appears influential in the defining of tyrosinase233-247IPYWDWRDAEKCDIC peptide epitopicity.
Related Concept Videos
Antigens Involved in Adaptive Immunity
Complete Antigens
Complete antigens possess both immunogenicity and reactivity.
Antigen Processing Pathways
MHC Class I: Presenting Endogenous...
Receptor Downregulation in MVBs
The EGFR can initiate signaling pathways that lead to cell proliferation, migration, and differentiation. Overexpression of EGFR stimulates cells to proliferate. Excessive EGFR activation may...
Translocation of Proteins into the Mitochondria
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Export of Misfolded Proteins out of the ER

