Crystal Structure of TIR Domain of TLR6 Reveals Novel Dimeric Interface of TIR-TIR Interaction for Toll-Like Receptor Signaling Pathway

Title
Crystal Structure of TIR Domain of TLR6 Reveals Novel Dimeric Interface of TIR-TIR Interaction for Toll-Like Receptor Signaling Pathway
Author(s)
박현호장태호
Keywords
NF-KAPPA-B; INNATE IMMUNITY; MOLECULAR REPLACEMENT; TRANSDUCTION; RECOGNITION; FAMILY; ADAPTERS; MYD88; DEATH; MODEL
Issue Date
201409
Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
Citation
JOURNAL OF MOLECULAR BIOLOGY, v.426, no.19, pp.3305 - 3313
Abstract
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.
URI
http://hdl.handle.net/YU.REPOSITORY/30827http://dx.doi.org/10.1016/j.jmb.2014.07.024
ISSN
0022-2836
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이과대학 > 화학생화학부 > Articles
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