A Structural Change in Butyrophilin upon Phosphoantigen Binding Underlies Phosphoantigen-Mediated VÎ³9VÎ´2 T Cell Activation.
Yang, Yunyun; Li, Liping; Yuan, Linjie; Zhou, Xiaoying; Duan, Jianxin; Xiao, Hongying; Cai, Ningning; Han, Shuai; Ma, Xianqiang; Liu, Weidong; Chen, Chun-Chi; Wang, Lingle; Li, Xin; Chen, Jiahuan; Kang, Ning; Chen, Jing; Shen, Zhixun; Malwal, Satish R; Liu, Wanli; Shi, Yan; Oldfield, Eric; Guo, Rey-Ting; Zhang, Yonghui.
; 50(4): 1043-1053.e5, 2019 Apr 16.
Artigo em Inglês | MEDLINE | ID: mdl-30902636
Epithelia Use Butyrophilin-like Molecules to Shape Organ-Specific Î³Î´ T Cell Compartments.
Phosphoantigen-induced conformational change of butyrophilin 3A1 (BTN3A1) and its implication on VÎ³9VÎ´2 T cell activation.
Regulation of Immunity by Butyrophilins.
The butyrophilin 3A1 intracellular domain undergoes a conformational change involving the juxtamembrane region.
Butyrophilin 3A (BTN3A, CD277)-specific antibody 20.1 differentially activates VÎ³9VÎ´2 TCR clonotypes and interferes with phosphoantigen activation.
The Juxtamembrane Domain of Butyrophilin BTN3A1 Controls Phosphoantigen-Mediated Activation of Human VÎ³9VÎ´2 T Cells.
The intracellular B30.2 domain of butyrophilin 3A1 binds phosphoantigens to mediate activation of human VÎ³9VÎ´2 T cells.
BTN3A1 Discriminates Î³Î´ T Cell Phosphoantigens from Nonantigenic Small Molecules via a Conformational Sensor in Its B30.2 Domain.