Effect of a Constitutively Active Mutation in the Transmembrane Region on Its Structure of the Juxtamembrane Region of the ErbB Receptor

摘要

ErbB receptors are member of the receptor tyrosine kinases and its functional disorder is a matter of concern in cancer. ErbB2/Neu has constitutively active mutation in transmembrane region and its structure must indicate the active state. Here we describe structural studies on the transmembrane-juxtamembrane sequence using solid-state NMR and fluorescence measurements. Our results have shown differences, for the wild type and the mutant, in dimer structure and behavior of juxtamembrane region as an addition PIP2 in the system.