Complement factor 5a receptor chimeras reveal the importance of lipid-facing residues in transport competence.

ABSTRACT: Residues that mediate helix-helix interactions within the seven transmembranes (TM) of G protein-coupled receptors are important for receptor biogenesis and the receptor switch mechanism. By contrast, the residues directly contacting the lipid bilayer have only recently garnered attention as potential receptor dimerization interfaces. In the present study, we aimed to determine the contributions of these lipid-facing residues to receptor function and oligomerization by systemically generating chimeric complement factor 5a receptors in which the entire lipid-exposed surface of a single TM helix was exchanged with the cognate residues from the angiotensin type 1 receptor. Disulfide-trapping and bioluminescence resonance energy transfer (BRET) studies demonstrated robust homodimerization of b

SUBMITTER: Klco JM 

PROVIDER: S-EPMC2747494 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature