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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 3 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 15N, 13C, and 1H 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. Biological context MyD88 is an essential and universal cytosolic adaptor protein in the signal transduction pathways mediated by members of the IL-1 family, including IL-18, and the Toll-like receptors (TLRs). It consists of an N-terminal death domain,