Identification of a Salt Bridge That Is Functionally Important for Chemokine Receptor CXCR1 but not CXCR2.

ABSTRACT: CXC chemokine receptors 1 (CXCR1) and 2 (CXCR2) have high sequence similarity and overlapping chemokine ligand profiles. Residue positions 3.32 and 7.39 are critical for signal transduction in the related CXCR4, and in these positions CXCR1 and CXCR2 contain oppositely charged residues (Lys^3.32 and Glu^7.39). Experimental and computed receptor structures reveal the possible formation of a salt bridge between transmembrane (TM) helices 3 and 7 via these two residues. To investigate the functional importance of Lys117^3.32 and Glu291^7.39 in CXCR1, along with the flanking Glu118^3.33, we performed a signaling study on 16 CXCR1 mutants using two different CXCL8 isoforms. While single Ala-mutation (K117^3.32A, E291^7.39A) a

SUBMITTER: Vabeno J 

PROVIDER: S-EPMC10425996 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature