| Literature DB >> 28337984 |
Xingdong Guo1, Chengsong Yan1, Hua Li1, Wenmao Huang2, Xiaoshan Shi1, Min Huang1, Yingfang Wang1, Weiling Pan1, Mingjun Cai3, Lunyi Li1, Wei Wu1, Yibing Bai1, Chi Zhang1, Zhijun Liu1, Xinyan Wang1, Xiaohui F Zhang4, Chun Tang5, Hongda Wang3, Wanli Liu6, Bo Ouyang1, Catherine C Wong1, Yi Cao2, Chenqi Xu1,7.
Abstract
T-cell receptor-CD3 complex (TCR) is a versatile signaling machine that can initiate antigen-specific immune responses based on various biochemical changes of CD3 cytoplasmic domains, but the underlying structural basis remains elusive. Here we developed biophysical approaches to study the conformational dynamics of CD3ε cytoplasmic domain (CD3εCD). At the single-molecule level, we found that CD3εCD could have multiple conformational states with different openness of three functional motifs, i.e., ITAM, BRS and PRS. These conformations were generated because different regions of CD3εCD had heterogeneous lipid-binding properties and therefore had heterogeneous dynamics. Live-cell imaging experiments demonstrated that different antigen stimulations could stabilize CD3εCD at different conformations. Lipid-dependent conformational dynamics thus provide structural basis for the versatile signaling property of TCR.Entities:
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Year: 2017 PMID： 28337984 PMCID： PMC5385618 DOI： 10.1038/cr.2017.42
Source DB: PubMed Journal: Cell Res ISSN： 1001-0602 Impact factor: 25.617