CDR3 loop flexibility contributes to the degeneracy of TCR recognition
JB Reiser, C Darnault, C Grégoire, T Mosser… - Nature …, 2003 - nature.com
JB Reiser, C Darnault, C Grégoire, T Mosser, G Mazza, A Kearney, PA van der Merwe…
Nature immunology, 2003•nature.comT 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-2Kb major histocompatibility complex molecule at a 2.7 Å resolution, and compared it
with the BM3. 3 TCR bound to the H-2Kb molecule loaded with a peptide that has no primary
sequence identity with VSV8. Comparison of these structures showed that the BM3. 3 TCR …
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-2Kb major histocompatibility complex molecule at a 2.7 Å resolution, and compared it
with the BM3. 3 TCR bound to the H-2Kb molecule loaded with a peptide that has no primary
sequence identity with VSV8. Comparison of these structures showed that the BM3. 3 TCR …
Abstract
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-2Kb major histocompatibility complex molecule at a 2.7 Å resolution, and compared it with the BM3.3 TCR bound to the H-2Kb 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) 3α could undergo rearrangements to adapt to structurally different peptide residues. Therefore, CDR3 loop flexibility helps explain TCR binding cross-reactivity.
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