2JXB

Structure of CD3epsilon-Nck2 first SH3 domain complex

2JXB の概要

• エントリーDOI: 10.2210/pdb2jxb/pdb
• 分子名称: T-cell surface glycoprotein CD3 epsilon chain, Cytoplasmic protein NCK2 (1 entity in total)
• 機能のキーワード: nck, cd3epsilon, t-cell receptor, sh3 domain, immunology, cytoplasm, sh2 domain, signaling protein complex
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P07766
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10267.66

構造登録者

Takeuchi, K.,Yang, H.,Ng, E.,Park, S.,Sun, Z.J.,Reinherz, E.L.,Wagner, G. (登録日: 2007-11-09, 公開日: 2008-09-23, 最終更新日: 2024-05-29)

主引用文献

Takeuchi, K.,Yang, H.,Ng, E.,Park, S.Y.,Sun, Z.Y.,Reinherz, E.L.,Wagner, G.
Structural and functional evidence that Nck interaction with CD3epsilon regulates T-cell receptor activity.
J.Mol.Biol., 380:704-716, 2008

PubMed Abstract: Recruitment of signaling molecules to the cytoplasmic domains of the CD3 subunits of the T-cell receptor (TCR) is crucial for early T-cell activation. These transient associations either do or do not require tyrosine phosphorylation of CD3 immune tyrosine activation motifs (ITAMs). Here we show that the non-ITAM-requiring adaptor protein Nck forms a complex with an atypical PxxDY motif of the CD3epsilon tail, which encompasses Tyr166 within the ITAM and a TCR endocytosis signal. As suggested by the structure of the complex, we find that Nck binding inhibits phosphorylation of the CD3epsilon ITAM by Fyn and Lck kinases in vitro. Moreover, the CD3epsilon-Nck interaction downregulates TCR surface expression upon physiological stimulation in mouse primary lymph node cells. This indicates that Nck performs an important regulatory function in T lymphocytes by inhibiting ITAM phosphorylation and/or removing cell surface TCR via CD3epsilon interaction.

PubMed: 18555270
DOI: 10.1016/j.jmb.2008.05.037

実験手法

SOLUTION NMR