1H, 13C, and 15N resonance assignment of the TIR domain of human MyD88.

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 Assign

authors

Ohnishi H,Tochio H,Kato Z,Kimura T,Hiroaki H,Kondo N,Shirakawa M

doi

10.1007/s12104-010-9222-0

subject

Has Abstract

pub_date

2010-10-01 00:00:00

pages

123-5

issue

2

eissn

1874-2718

issn

1874-270X

journal_volume

4

pub_type

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