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Updated: Aug 11, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
Membrane proteins which exhibit multiple topological orientations
1University of Southern California, School of Medicine, Department of Biochemistry and Molecular Biology, Los Angeles 90033, USA.
Abstract:
Membrane protein folding patterns can be divided into several classes based on their orientation and the topogenic sequences that regulate their insertion into the ER membrane. The orientation of membrane proteins is regulated by charge distribution in the polypeptide chain as well folding characteristics of the N-terminal domain. Protein targeting characteristic are determined by several sequence motifs found in the C- and N-terminal domains as well as by oligomerization. Several proteins, such as Pgp, ductin, CP450s and mEH, have been shown to exhibit more than one topological orientation in the ER which can result in protein targeting to more than one cell compartment as well as the expression of multiple biological functions.
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