Journal article

The production, purification and crystallization of a soluble heterodimeric form of a highly selected T-cell receptor in its unliganded and liganded state

CS Clements, L Kjer-Nielsen, WA MacDonald, AG Brooks, AW Purcell, J McCluskey, J Rossjohn

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | INT UNION CRYSTALLOGRAPHY | Published : 2002

Abstract

T-cell antigen receptors (TcRs) are heterodimeric cell-surface receptors that play a pivotal role in the cellular immune response. The TcR interacts specifically with a peptide-laden major histocompatability complex (pMHC). A human TcR has been characterized that interacts with an immunodominant epitope, FLRGRAYGL, from the Epstein-Barr virus, a ubiquitous human pathogen, in complex with HLA-B8. Despite the vast TcR repertoire, this TcR is found in up to 10% of the total T-cell population in seropositive HLA-B8+ individuals. In this report, this highly selected TcR is characterized by expressing in Escherichia coli, refolding, purifying and crystallizing the receptor. In addition, the HLA-B8..

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