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Title:Characterization of a T Cell Receptor: Peptide/MHC Binding Interaction
Author(s):Schlueter, Carol Joy
Doctoral Committee Chair(s):Kranz, David M.
Department / Program:Biochemistry
Discipline:Biochemistry
Degree Granting Institution:University of Illinois at Urbana-Champaign
Degree:Ph.D.
Genre:Dissertation
Subject(s):Health Sciences, Immunology
Abstract:To begin to examine the 2C TCR residues which provide a significant thermodynamic contribution toward the binding energy of a variety of ligands, including monoclonal antibodies (mAb), superantigens, and peptide/MHC ligands, we have expressed a family of 2C scTCRs which contain alanine point mutations in the complementarity determining regions (CDR) and fourth hypervariable region of the $\beta$ chain. Using these mutant scTCRs, we have identified V$\beta$ residues which are energetically important in the interaction of the 2C TCR with the anti-V$\beta$8 mAb F23.2, the anti-clonotypic mAb 1B2, and the peptide/MHC ligand QL9/L$\rm\sp{d}.$ Residues from all three CDR$\beta$ loops were implicated in the binding of the 2C TCR to QL9/L$\rm\sp{d}.$ Furthermore, every residue identified as part of the QL9/L$\rm\sp{d}$ epitope was also identified as part of the 1B2 epitope, suggesting that these two TCR ligands may share certain features in their tertiary structure even though their primary and secondary sequences are quite different. The construction of this panel of V$\beta$ mutant scTCRs has also facilitated possible future identification of 2C TCR $\beta$ chain residues which contact other peptide/MHC, mAb, and superantigen ligands.
Issue Date:1997
Type:Text
Language:English
Description:268 p.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1997.
URI:http://hdl.handle.net/2142/84886
Other Identifier(s):(MiAaPQ)AAI9737243
Date Available in IDEALS:2015-09-25
Date Deposited:1997


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