1H, 13C, and 15N resonance assignment of the TIR domain of human MyD88.
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.
Ohnishi
Hidenori
H
Department of Pediatrics, Graduate School of Medicine, Gifu University, Yanagido 1-1, Gifu, 501-1194, Japan. ohnishih@gifu-u.ac.jp
Tochio
Hidehito
H
Kato
Zenichiro
Z
Kimura
Takeshi
T
Hiroaki
Hidekazu
H
Kondo
Naomi
N
Shirakawa
Masahiro
M
D002247:Carbon Isotopes; D006801:Humans; D006859:Hydrogen; D053594:Myeloid Differentiation Factor 88 / Q000737:chemistry*; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary
D002247:Carbon Isotopes; D053594:Myeloid Differentiation Factor 88; D009587:Nitrogen Isotopes; D006859:Hydrogen