The CD3 molecule is a critical component of both humoral and cellular immune responses, and yet while the structure and molecular assembly of other key mediators such as CD4 and CD8 have been reported, individual CD3 subunits have not been well characterized. Our understanding of the manner in which they interact remains limited, and the question of how many subunits are required for a functional CD3 molecular complex is yet to be addressed. It has been suggested that CD3ε pairs with CD3γ or with CD3δ, forming CD3εγ and CD3εδ heterodimers that associate with α/β T cell receptors (TCRs) and CD3 ζ 2 dimers. In this study we investigated whether interactions between each CD3ε subunit play a role in the formation of the CD3 molecular complex. Our results revealed that the human CD3ε subunit forms a homodimer structure, which is a crucial piece of information for the elucidation of cellular signaling following TCR receptor ligation, and provide insight into our understanding of the molecular assembly of the CD3 molecular complex.

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