GEC1-kappa opioid receptor binding involves hydrophobic interactions: GEC1 has chaperone-like effect.

ABSTRACT: We demonstrated previously that the protein GEC1 (glandular epithelial cell 1) bound to the human kappa opioid receptor (hKOPR) and promoted cell surface expression of the receptor by facilitating its trafficking along the secretory pathway. Here we showed that three hKOPR residues (Phe345, Pro346, and Met350) and seven GEC1 residues (Tyr49, Val51, Leu55, Thr56, Val57, Phe60, and Ile64) are indispensable for the interaction. Modeling studies revealed that the interaction was mediated via direct contacts between the kinked hydrophobic fragment in hKOPR C-tail and the curved hydrophobic surface in GEC1 around the S2 beta-strand. Intramolecular Leu44-Tyr109 interaction in GEC1 was important, likely by maintaining its structural integrity. Microtubule binding mediated by the GEC1 N-terminal do

SUBMITTER: Chen Y 

PROVIDER: S-EPMC2615498 | biostudies-literature | 2009 Jan

REPOSITORIES: biostudies-literature