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The structure of the CD3ζζ transmembrane dimer in lipid bilayers

Abstract : 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.
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Soumis le : mercredi 17 mars 2021 - 10:53:20
Dernière modification le : jeudi 15 avril 2021 - 11:22:02

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Satyan Sharma, Marc Lensink, André H. Juffer. The structure of the CD3ζζ transmembrane dimer in lipid bilayers. BBA - Biochimica et Biophysica Acta, Elsevier, 2014, Biochimica et biophysica acta, 1838 (3), pp.739-746. ⟨10.1016/j.bbamem.2013.12.001⟩. ⟨hal-03171753⟩



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