T Cell Receptor Alpha Chain Residues Involved in Antibody Binding and Recognition of peptide/MHC Ligand
Brodnicki, Thomas Charles
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https://hdl.handle.net/2142/84875
Description
Title
T Cell Receptor Alpha Chain Residues Involved in Antibody Binding and Recognition of peptide/MHC Ligand
Author(s)
Brodnicki, Thomas Charles
Issue Date
1997
Doctoral Committee Chair(s)
Kranz, David M.
Department of Study
Biochemistry
Discipline
Biochemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Health Sciences, Immunology
Language
eng
Abstract
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 $\alpha$ chain mutation, located within a loop that is analogous to the fourth hypervariable region (HV4) of the $\beta$ chain, disrupted binding to QL9/L$\sp{\rm d}$ approximately five-fold. Based on these results and a homology model of the 2C $\alpha$ 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.
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