T Cell Receptor Alpha Chain Residues Involved in Antibody Binding and Recognition of peptide/MHC Ligand

Mutant 2C scTCRs were further examined in ligand binding experiments. The 2C TCR recognizes a peptide (QL9) presented by the MHC product L$\sp{\rm d}$. Four alanine mutations which affected mAb binding also disrupted binding to the QL9/L$\sp{\rm d}$ complex by greater than ten-fold relative to the wild-type scTCR. A fifth α chain mutation, located within a loop that is analogous to the fourth hypervariable region (HV4) of the β chain, disrupted binding to QL9/L$\sp{\rm d}$ approximately five-fold. Based on these results and a homology model of the 2C α chain variable region, these five residues are likely to be involved in either stabilization of CDR loops or in direct contact with the peptide/MHC ligand.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Brodnicki, Thomas Charles

Contributors dc:contributor

• Kranz, David M.

• Health Sciences, Immunology

Language dc:language

eng

Identifier

(MiAaPQ)AAI9717257

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/84875