IL-1/Toll-like Receptor Superfamily 신호전달에 관여하는 TRAF6 결합 Motif의 규명

Abstract

Crystal structure of TRAF6 in complex with TRAF6-binding sites from CD4O was previously determined. The structure revealed a distinct TRAF6-binding groove of CD4O, the key structural determinant of interaction. The structural information leads to a proposed TRAF6-binding motif. This allows the identification of TRAF6-binding sequences in the hIRAK protein, whose functional requirement in IL-1/Toll-like eceptor superfamilies-mediated signal transduction is further demonstrated using site- directed mutagenesis. The mutational effects of MRAK on the down-stream NF-KB signaling shows the importance of the TRAF6 interface for signaling by IL-1/Toll-like receptor superfamilies.