Characterization of a computationally designed water-soluble human μ-opioid receptor variant using available structural information.

ABSTRACT:

Background

The recent X-ray crystal structure of the murine μ-opioid receptor (MUR) allowed the authors to reengineer a previously designed water-soluble variant of the transmembrane portion of the human MUR (wsMUR-TM).

Methods

The new variant of water-soluble MUR (wsMUR-TM_v2) was engineered based on the murine MUR crystal structure. This novel variant was expressed in Escherichia coli and purified. The properties of the receptor were characterized and compared with those of wsMUR-TM.

Results

Seven residues originally included for mutation in the design of the wsMUR-TM were reverted to their native identities. wsMUR-TM_v2 contains 16% mutations of the total sequence. It was overexpressed and purified with high yield. Although dimers and higher oligomers were observed

SUBMITTER: Zhao X 

PROVIDER: S-EPMC4175066 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature