Mutational analysis identifies residues crucial for homodimerization of myeloid differentiation factor 88 (MyD88) and for its function in immune cells

Maria Loiarro, Elisabetta Volpe, Vito Ruggiero, Grazia Gallo, Roberto Furlan, Chiara Maiorino, Luca Battistini, Claudio Sette

Research output: Contribution to journalArticle

Abstract

Background: MyD88 is an adaptor protein that plays a crucial role in the immune response. Results: We identified residues within the TIR domain of MyD88 required for protein self-association. Conclusion: Interference with the surface of homodimerization identified by these residues inhibits MyD88 function. Significance: The inhibition of MyD88 activity could be a good therapeutic strategy for inflammatory and autoimmune diseases.

Original languageEnglish
Pages (from-to)30210-30222
Number of pages13
JournalJournal of Biological Chemistry
Volume288
Issue number42
DOIs
Publication statusPublished - Oct 18 2013

    Fingerprint

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this