Structural Model of the Extracellular Assembly of the TCR-CD3 Complex.
Name:
Publisher version
View Source
Access full-text PDFOpen Access
View Source
Check access options
Check access options
Average rating
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Star rating
Your vote was cast
Thank you for your feedback
Thank you for your feedback
Author
Natarajan, AswinNadarajah, Vidushan
Felsovalyi, Klara
Wang, Wenjuan
Jeyachandran, Vivian R
Wasson, Riley A
Cardozo, Timothy
Bracken, Clay
Krogsgaard, Michelle
Journal title
Cell reportsDate Published
2016-03-17Publication Volume
14Publication Issue
12Publication Begin page
2833Publication End page
45
Metadata
Show full item recordAbstract
Antigen recognition of peptide-major histocompatibility complexes (pMHCs) by T cells, a key step in initiating adaptive immune responses, is performed by the T cell receptor (TCR) bound to CD3 heterodimers. However, the biophysical basis of the transmission of TCR-CD3 extracellular interaction into a productive intracellular signaling sequence remains incomplete. Here we used nuclear magnetic resonance (NMR) spectroscopy combined with mutational analysis and computational docking to derive a structural model of the extracellular TCR-CD3 assembly. In the inactivated state, CD3γε interacts with the helix 3 and helix 4-F strand regions of the TCR Cβ subunit, whereas CD3δε interacts with the F and C strand regions of the TCR Cα subunit in this model, placing the CD3 subunits on opposing sides of the TCR. This work identifies the molecular contacts between the TCR and CD3 subunits, identifying a physical basis for transmitting an activating signal through the complex.Citation
Natarajan A, Nadarajah V, Felsovalyi K, Wang W, Jeyachandran VR, Wasson RA, Cardozo T, Bracken C, Krogsgaard M. Structural Model of the Extracellular Assembly of the TCR-CD3 Complex. Cell Rep. 2016 Mar 29;14(12):2833-45. doi: 10.1016/j.celrep.2016.02.081. Epub 2016 Mar 17. PMID: 26997265; PMCID: PMC4902171.DOI
10.1016/j.celrep.2016.02.081ae974a485f413a2113503eed53cd6c53
10.1016/j.celrep.2016.02.081
Scopus Count
Collections
The following license files are associated with this item:
- Creative Commons
Except where otherwise noted, this item's license is described as Copyright © 2016 The Authors. Published by Elsevier Inc. All rights reserved.
Related articles
- Identification of the Docking Site for CD3 on the T Cell Receptor β Chain by Solution NMR.
- Authors: He Y, Rangarajan S, Kerzic M, Luo M, Chen Y, Wang Q, Yin Y, Workman CJ, Vignali KM, Vignali DA, Mariuzza RA, Orban J
- Issue date: 2015 Aug 7
- Structural basis of assembly of the human T cell receptor-CD3 complex.
- Authors: Dong D, Zheng L, Lin J, Zhang B, Zhu Y, Li N, Xie S, Wang Y, Gao N, Huang Z
- Issue date: 2019 Sep
- The structure of the zetazeta transmembrane dimer reveals features essential for its assembly with the T cell receptor.
- Authors: Call ME, Schnell JR, Xu C, Lutz RA, Chou JJ, Wucherpfennig KW
- Issue date: 2006 Oct 20
- The short length of the extracellular domain of zeta is crucial for T cell antigen receptor function.
- Authors: Minguet S, Swamy M, Schamel WW
- Issue date: 2008 Mar 15
- The protein interactions of the immunoglobulin receptor family tyrosine-based activation motifs present in the T cell receptor zeta subunits and the CD3 gamma, delta and epsilon chains.
- Authors: Osman N, Turner H, Lucas S, Reif K, Cantrell DA
- Issue date: 1996 May