期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 426, 期 19, 页码 3305-3313出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2014.07.024
关键词
crystal structure; TLR6; TIR domain; innate immunity; NF-kappaB
资金
- Basic Science Research Program through the National Research Foundation of Korea of the Ministry of Education, Science and Technology [2012R1A2A2A01010870]
- Korea Healthcare Technology R&D Project, Ministry of Health & Welfare, Republic of Korea [HI13C1449]
- National Research Foundation of Korea [2012R1A2A2A01010870] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Toll-like receptors (TLRs) are responsible for recognition of particular pathogens during the innate immune response and cytoplasmic Toll/interleukin-1 receptor (TIR) domain responsible for downstream signaling. TLR6 working with TLR2 can detect bacterial lipoprotein leading signal for nuclear factor-kappaB activation for immune response. To better understand TLR-mediated signaling event in the innate immune system, in this study, we report the first crystal structure of the TIR domain of TLR6 at 2.2 angstrom resolution. Our structure reveals novel homo-dimerization interfaces, which might be a critical for the interaction with TIR-containing adaptor proteins and itself. We also report structural similarities and differences of TLR6 with those of other TIR domains, which may be functionally relevant. (C) 2014 Elsevier Ltd. All rights reserved.
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