期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 138, 期 -, 页码 565-572出版社
ELSEVIER
DOI: 10.1016/j.ijbiomac.2019.07.139
关键词
Apoptosis; Innate immunity; Death domain superfamily; Protein-protein interaction; Structure; Domain swapping
资金
- Basic Science Research Program of the National Research Foundation of Korea (NRF) of the Ministry of Education, Science and Technology [NRF-2017M3A9D8062960, NRF-2018R1A2B2003635]
- Korea Healthcare Technology R&D Project, Ministry of Health and Welfare, Republic of Korea [HI17C0155]
The role of death domain (DD) protein-mediated inter-protein interactions in cell death and immune cell signaling have been extensively investigated as they are tentative targets for therapeutic interventions and are involved in signal transduction. Structural studies, especially those involving the recent advanced cryo-electron microscopy, indicated that the DD superfamily proteins can assemble into different forms of oligomers, including homo and heterodimer, honey comb-like circular oligomer, and helical filament via three types of interactions, namely type I, type II, and type III. Recently, several structural reports indicated that domain swapping mediated dimerization of the DD superfamily proteins might be an alternative oligomerization strategy in this family of protein interacting domains. In this review, all the binding strategies associated with the DD superfamily are summarized with a special focus on the novel domain swapping mechanism. (C) 2019 Elsevier B.V. All rights reserved.
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