Cannabinoid receptor interacting protein 1a interacts with myristoylated Gα_i N terminus via a unique gapped β-barrel structure.

ABSTRACT: Cannabinoid receptor interacting protein 1a (CRIP1a) modulates CB₁ cannabinoid receptor G-protein coupling in part by altering the selectivity for Gα_i subtype activation, but the molecular basis for this function of CRIP1a is not known. We report herein the first structure of CRIP1a at a resolution of 1.55 Å. CRIP1a exhibits a 10-stranded and antiparallel β-barrel with an interior comprised of conserved hydrophobic residues and loops at the bottom and a short helical cap at the top to exclude solvent. The β-barrel has a gap between strands β8 and β10, which deviates from β-sandwich fatty acid-binding proteins that carry endocannabinoid compounds and the Rho-guanine nucleotide dissociation inhibitor predicted by computational threading algorithms. The structural homolo

SUBMITTER: Booth WT 

PROVIDER: S-EPMC8446797 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature