Christopher Koch Butler University
Faculty Sponsor(s): Mark Macbeth Butler UniversityThe Sigma-1 receptor (S1R) is an important pharmaceutical target that has been linked to several neurological diseases and drug addiction. The S1R typically occurs as a trimer, which is a protein bound to two identical proteins. It has been proposed this multimerization is important for attenuating interactions with the dopamine transporter (DAT). When a substance is present it either promotes the S1R stay in the trimer form or for the S1R to dissociate into a monomer form. The monomer form is necessary to interact with the DAT. This project aims to assess the structure and activity of the mammalian Sigma-1 receptor (S1R). A truncated form of the receptor and the E102Q variant, which displays altered activity and cellular localization, will be expressed, purified and crystallized in order to determine their contributions to the overall structure. Additionally, binding studies using radioactive ligands of the receptor will be performed to assess the activity of the mutant S1Rs.
When & Where
Irwin Library 1st Floor