In vitro assembly complex formation of TRAIP CC and RAP 80 zinc finger motif revealed by our study.

ABSTRACT:

Background

Tumor necrosis factor interacting protein (TRAIP/TRIP) is an important cell-signaling molecule that prevents the TNF-induced-nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) activation via direct interaction with TRAF 2 protein. TRAIP is a crucial downstream signaling molecule, implicated in several signaling pathways. Due to these multifunctional effects, TRAIP is more related to cellular mitosis, chromosome segregation, and DNA damage response. Tumor necrosis factor interacting protein is a downstream signaling molecule that contains a RING domain with E3 ubiquitin ligase activity at the N terminal side followed by coiled-coil and C terminal leucine zipper domain. Human TRAIP is constituted of 469 amino acids with 76% sequence similarity wi

SUBMITTER: Bhat EA 

PROVIDER: S-EPMC8626312 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature