Structural basis for the differential interaction of Scribble PDZ domains with the guanine nucleotide exchange factor β-PIX.

ABSTRACT: Scribble is a highly conserved protein regulator of cell polarity that has been demonstrated to function as a tumor suppressor or, conversely, as an oncogene in a context-dependent manner, and it also controls many physiological processes ranging from immunity to memory. Scribble consists of a leucine-rich repeat domain and four PDZ domains, with the latter being responsible for most of Scribble's complex formation with other proteins. Given the similarities of the Scribble PDZ domain sequences in their binding grooves, it is common for these domains to show overlapping preferences for the same ligand. Yet, Scribble PDZ domains can still exhibit unique binding profiles toward other ligands. This raises the fundamental question as to how these PDZ domains discriminate ligands and exert spec

SUBMITTER: Lim KYB 

PROVIDER: S-EPMC5733582 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature