Energetics and Structure Prediction of the Network of Homo- and Hetero- Oligomers Formed by the Transmembrane Domains of the ErbReceptor Family of Proteins

摘要

The erbB/HER receptor proteins use a single transmembrane domain to mediate growth factor induced signal transduction across membranes. A complex network of both homo- and hetero-oligomeric interactions exists for the members of this receptor family. The goals of our research are to examine the role played by the transmembrane domain in this network of interactions. We have measured the energetics of homo- and hetero-oligomerization for the four human erbB transmembrane domains. We find all interactions to be modest in energy. We have developed a thermodynamic model to distinguish random interactions of proteins in micelles from preferential ones. We propose that the erbB transmembrane domains do not require strong preferential interactions in order to enhance the interaction propensity for a covalently bound soluble domain.