The structural basis for Her2's role as a dedicated heterodimerization partner for other EGFR family receptors is elucidated with long-timescale atomistic simulations.

Regions outside the major receptor binding interface of DLL1 and DLL4 contribute to context-dependent divergence of ligand function in vivo and differential Notch1 and Notch2 activation in vitro.

VAR2CSA, the leading candidate antigen for a placental malaria vaccine, displays epitopes targeted by naturally acquired broadly neutralizing antibodies of African multigravidae.

Structural, biophysical, and functional analyses reveal that mutations in TREM2 trigger either misfolding or reduced binding to cell-surface glycosaminoglycans, which segregate with neurodegenerative disease link and highlight a functional surface linked to the pathogenesis of Alzheimer's disease.

The ectodomain of the human polymeric Ig receptor maintains a closed triangular shape that binds and excludes bacteria in mucosa, or opens to bind and transport polymeric Ig ligands across epithelial cells.

The crystal structure of neutralizing antibody AR3X in complex with HCV E2 glycoprotein reveals unusual features of antibody recognition in which a conserved epitope is recognized by distinct antibody poses.

A viral fusogen drives cell-cell fusion by hijacking the actin machinery to directly couple actin assembly with a short fusogenic ectodomain.

Cryo-EM structures uncover glycosylation in the ectodomains of full-length HER4 homodimer and HER2/HER4 heterodimer complexes, revealing how the binding of various growth factors alters dynamics at the dimerization interface.

A single-nucleotide I232T polymorphic change in FcγRIIB's transmembrane domain bends FcγRIIB's ectodomains toward cell membrane to allosterically hinder FcγRIIB's ligand association, providing novel molecular mechanism for functional loss of FcγRIIB-I232T.

Ligand binding induces DDR1 kinase activity through recruitment of DDR1 receptors into signalling clusters in which phosphorylation occurs across different dimers.