| Literature DB >> 20354830 |
Hidenori Ohnishi1, Hidehito Tochio, Zenichiro Kato, Takeshi Kimura, Hidekazu Hiroaki, Naomi Kondo, Masahiro Shirakawa.
Abstract
Myeloid differentiating factor 88 (MyD88) is one of a critical adaptor molecule in the Toll-like receptor (TLR) signaling pathway. The TIR domain of MyD88 serves as a protein-protein interaction module and interacts with other TIR-containing proteins such as Mal (MyD88 adaptor-like) and Toll-like receptor 4 to form signal initiation complexes. Here we report the (15)N, (13)C, and (1)H chemical shift assignments of the TIR domain of MyD88. The resonance assignments obtained in this work will contribute to the study of heteromeric TIR-TIR interactions between MyD88 and TIR-containing receptors or adaptors.Entities:
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Year: 2010 PMID： 20354830 DOI： 10.1007/s12104-010-9222-0
Source DB: PubMed Journal: Biomol NMR Assign ISSN： 1874-270X Impact factor: 0.746