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.
journal_name
Biomol NMR Assignjournal_title
Biomolecular NMR assignmentsauthors
Ohnishi H,Tochio H,Kato Z,Kimura T,Hiroaki H,Kondo N,Shirakawa Mdoi
10.1007/s12104-010-9222-0subject
Has Abstractpub_date
2010-10-01 00:00:00pages
123-5issue
2eissn
1874-2718issn
1874-270Xjournal_volume
4pub_type
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