Functional binding of E-selectin to its ligands is enhanced by structural features beyond its lectin domain.

ABSTRACT: Selectins are key to mediating interactions involved in cellular adhesion and migration, underlying processes such as immune responses, metastasis, and transplantation. Selectins are composed of a lectin domain, an epidermal growth factor (EGF)-like domain, multiple short consensus repeats (SCRs), a transmembrane domain, and a cytoplasmic tail. It is well-established that the lectin and EGF domains are required to mediate interactions with ligands; however, the contributions of the other domains in mediating these interactions remain obscure. Using various E-selectin constructs produced in a newly developed silkworm-based expression system and several assays performed under both static and physiological flow conditions, including flow cytometry, glycan array analysis, surface plasmon reson

SUBMITTER: Aleisa FA 

PROVIDER: S-EPMC7076219 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature