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RSS FeedsConformational flexibility and inhibitor binding to unphosphorylated interleukin-1 receptor-associated kinase 4 (IRAK4) [Protein Structure and Folding] (Journal of Biological Chemistry)

 
 

22 march 2019 09:00:41

 
Conformational flexibility and inhibitor binding to unphosphorylated interleukin-1 receptor-associated kinase 4 (IRAK4) [Protein Structure and Folding] (Journal of Biological Chemistry)
 


Interleukin-1 receptor-associated kinase 4 (IRAK4) is a key player in innate immune and inflammatory responses, performing a critical role in signal transduction downstream of Toll-like receptors and interleukin-1 (IL-1) receptors. Upon ligand binding and via its N-terminal death domain, IRAK4 is recruited to an oligomeric receptor that is proximal to the Myddosome signaling complex, inducing IRAK4 kinase domain dimerization, autophosphorylation, and activation. To date, all known IRAK4 structures are in the active conformation, precluding a good understanding of IRAK4`s conformational dynamics. To address this issue, here we first solved three crystal structures of the IRAK4 kinase domain (at


 
80 viewsCategory: Biochemistry
 
Influence of the N-terminal segment and the PHY-tongue element on light-regulation in bacteriophytochromes [Protein Structure and Folding] (Journal of Biological Chemistry)
Synergy among non-desmoglein antibodies contributes to the immunopathology of desmoglein antibody-negative pemphigus vulgaris [Cell Biology] (Journal of Biological Chemistry)
 
 
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