The leukotriene B₄ receptor BLT1 is stabilized by transmembrane helix capping mutations.

ABSTRACT: In this study, we introduced structure-based rational mutations in the guinea pig leukotriene B₄ receptor (gpBLT1) in order to enhance the stabilization of the protein. Elements thought to be unfavorable for the stability of gpBLT1 were extracted based on the stabilization elements established in soluble proteins, determined crystal structures of G-protein-coupled receptors (GPCRs), and multiple sequence alignment. The two unfavorable residues His83^2.67 and Lys88^3.21, located at helix capping sites, were replaced with Gly (His83Gly^2.67 and Lys88Gly^3.21). The modified protein containing His83Gly^2.67/Lys88Gly^3.21 was highly expressed, solubilized, and purified and exhibited improved thermal stability by 4 °C in comp

SUBMITTER: Hori T 

PROVIDER: S-EPMC5668910 | biostudies-literature | 2015 Dec

REPOSITORIES: biostudies-literature