期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2004
卷号：101
期号：20
页码：7675-7680
DOI：10.1073/pnas.0402295101
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The CD3{epsilon}{gamma} heterodimer is essential for expression and function of the T cell receptor. The crystal structure of the human CD3{epsilon}{gamma} heterodimer is described to 2.1-A resolution complexed with OKT3, a therapeutic mAb that not only activates and tolerizes mature T cells but also induces regulatory T cells. The mode of CD3{epsilon}{gamma} dimerization provides a general structural basis for CD3 assembly and maps candidate T cell antigen receptor docking sites, including a duplicated linear region rich in acidic residues that is unique to human CD3{epsilon}. OKT3 binds to an atypically small area of CD3{epsilon} and has a low affinity for the isolated CD3{epsilon}{gamma} heterodimer. The structure of the OKT3/CD3{epsilon}{gamma} complex has implications for T cell signaling and therapeutic design.
