Virtually every aspect of the human adaptive immune response is controlled by T cells. The T cell receptor (TCR) complex is responsible for the recognition of foreign peptide sequences, forming the initial step in the elimination of germ-infected cells. The recognition leads to an extracellular conformational change that is transmitted intracellularly through the Cluster of Differentiation 3 (CD3) subunits of the TCR-CD3 complex. Here we address the interplay between the disulfide-linked CD3ζζ dimer, an essential signaling component of the TCR-CD3 complex, and its lipidic environment. The disulfide bond formation requires the absolute presence of a nearby conserved aspartic acid, a fact that has mystified the scientific community. We use atomistic simulation methods to demonstrate that the conserved aspartic acid pair of the CD3ζζ dimer leads to a deformation of the membrane. This deformation changes the local environment of the cysteines and promotes disulfide bond formation. We also investigate the role of a conserved Tyr, highlighting its possible role in the interaction with other transmembrane components of the TCR-CD3 complex.