Structural basis for CD97 recognition of the decay-accelerating factor CD55 suggests mechanosensitive activation of adhesion GPCRs.

ABSTRACT: The adhesion G protein-coupled receptor CD97 and its ligand complement decay-accelerating factor CD55 are important binding partners in the human immune system. Dysfunction in this binding has been linked to immune disorders such as multiple sclerosis and rheumatoid arthritis, as well as various cancers. Previous literatures have indicated that the CD97 includes 3 to 5 epidermal growth factor (EGF) domains at its N terminus and these EGF domains can bind to the N-terminal short consensus repeat (SCR) domains of CD55. However, the details of this interaction remain elusive, especially why the CD55 binds with the highest affinity to the shortest isoform of CD97 (EGF_1,2,5). Herein, we designed a chimeric expression construct with the EGF_1,2,5 domains of CD97 and the SCR<

SUBMITTER: Niu M 

PROVIDER: S-EPMC8191316 | biostudies-literature | 2021 Jan-Jun

REPOSITORIES: biostudies-literature