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T cell receptor (TCR) binding degeneracy lies at the heart of several physiological and pathological phenomena, yet its structural basis is poorly understood. We determined the crystal structure of a complex involving the BM3.3 TCR and an octapeptide (VSV8) bound to the H-2K(b) major histocompatibility complex molecule at a 2.7 A resolution, and compared it with the BM3.3 TCR bound to the H-2K(b) molecule loaded with a peptide that has no primary sequence identity with VSV8. Comparison of these structures showed that the BM3.3 TCR complementarity-determining region (CDR) 3alpha could undergo rearrangements to adapt to structurally different peptide residues. Therefore, CDR3 loop flexibility helps explain TCR binding cross-reactivity.

Original publication

DOI

10.1038/ni891

Type

Journal article

Journal

Nat Immunol

Publication Date

03/2003

Volume

4

Pages

241 - 247

Keywords

Complementarity Determining Regions, Humans, Ligands, Protein Binding, Protein Conformation, Protein Structure, Tertiary, Receptors, Antigen, T-Cell, Structure-Activity Relationship, T-Lymphocytes