English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

The Na + , K + -ATPase transports Na + and K + across the membrane of all animal cells. In addition to its ion transporting function, the Na + , K + -ATPase acts as a homotypic epithelial cell adhesion molecule via its β 1 subunit. The extracellular region of the Na + , K + -ATPase β 1 subunit includes a single globular immunoglobulin-like domain. We performed Molecular Dynamics simulations of the ectodomain of the β 1 subunit and a refined protein-protein docking prediction. Our results show that the β 1 subunit Ig-like domain maintains an independent structure and dimerizes in an antiparallel fashion. Analysis of the putative interface identified segment Lys221-Tyr229. We generated triple mutations on YFP-β 1 subunit fusion proteins to assess the contribution of these residues. CHO fibroblasts transfected with mutant β 1 subunits showed a significantly decreased cell-cell adhesion. Association of β 1 subunits in vitro was also reduced, as determined by pull-down assays. Altogether, we conclude that two Na + , K + -ATPase molecules recognize each other by a large interface spanning residues 221-229 and 198-207 on their β 1 subunits.

A Model for the Homotypic Interaction between Na+,K+-ATPase β1 Subunits Reveals the Role of Extracellular Residues 221–229 in Its Ig-Like Domain