Title :

The structure of the CD3ζζ transmembrane dimer in lipid bilayers

Author(s) :

Sharma, Satyan [Auteur]
University of Oulu
Lensink, Marc [Auteur]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Juffer, André H. [Auteur]
University of Oulu

Journal title :

Biochimica et biophysica acta

Abbreviated title :

Biochim. Biophys. Acta

Volume number :

1838

Pages :

739-746

Publication date :

2014-03

ISSN :

0006-3002

English keyword(s) :

Cell Membrane
T cell receptor
Lipid Bilayers
Humans
CD3 Complex
Protein Multimerization
CD3ζζ transmembrane domain
Models, Molecular
Molecular dynamics
Protein Conformation
TCR–CD3 complex
Protein Folding

HAL domain(s) :

Chimie/Chimie théorique et/ou physique

English abstract : [en]

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 ...
Show more >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.Show less >

Language :

Anglais

Audience :

Non spécifiée

Administrative institution(s) :

CNRS
Université de Lille

Collections :

• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Research team(s) :

Computational Molecular Systems Biology

Submission date :

2020-02-12T15:11:15Z
2021-03-17T09:53:15Z