Ontology highlight
ABSTRACT:
SUBMITTER: Yung YL
PROVIDER: S-EPMC4583037 | biostudies-literature | 2015 Sep
REPOSITORIES: biostudies-literature
Yung Yuk-Lin YL Cheung Ming-Yan MY Miao Rui R Fong Yu-Hang YH Li Kwan-Pok KP Yu Mei-Hui MH Chye Mee-Len ML Wong Kam-Bo KB Lam Hon-Ming HM
The Journal of biological chemistry 20150818 39
The C2 domain is one of the most diverse phospholipid-binding domains mediating cellular signaling. One group of C2-domain proteins are plant-specific and are characterized by their small sizes and simple structures. We have previously reported that a member of this group, OsGAP1, is able to alleviate salt stress and stimulate defense responses, and bind to both phospholipids and an unconventional G-protein, OsYchF1. Here we solved the crystal structure of OsGAP1 to a resolution of 1.63 Å. Using ...[more]