Ontology highlight
ABSTRACT:
SUBMITTER: Hu F
PROVIDER: S-EPMC4646294 | biostudies-literature | 2015 Oct
REPOSITORIES: biostudies-literature
Hu Fen F Shi Xiaoli X Li Bowen B Huang Xiaochen X Morelli Xavier X Shi Ning N
The Journal of biological chemistry 20150911 44
GM130 and GRASP65 are Golgi peripheral membrane proteins that play a key role in Golgi stacking and vesicle tethering. However, the molecular details of their interaction and their structural role as a functional unit remain unclear. Here, we present the crystal structure of the PDZ domains of GRASP65 in complex with the GM130 C-terminal peptide at 1.96-Å resolution. In contrast to previous findings proposing that GM130 interacts with GRASP65 at the PDZ2 domain only, our crystal structure of the ...[more]