CDR3 loop flexibility contributes to the degeneracy of TCR recognition.

CDR3 loop flexibility contributes to the degeneracy of TCR recognition.

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 histocompatibil...

ver descrição completa

Detalhes bibliográficos
Principais autores: Reiser, J, Darnault, C, Grégoire, C, Mosser, T, Mazza, G, Kearney, A, Van Der Merwe, P, Fontecilla-Camps, J, Housset, D, Malissen, B
Formato: Journal article
Idioma:English
Publicado em: 2003
Descrição
Resumo: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.

Registros relacionados