Structure of the heterophilic interaction between the nectin-like 4 and nectin-like 1 molecules.

ABSTRACT: Nectin-like (Necl) molecules are Ca²⁺-independent Ig-like transmembrane cell adhesion molecules that participate in junctions between different cell types. The specific cell-cell adhesions mediated by Necl proteins are important in neural development and have been implicated in neurodegenerative diseases. Here, we present the crystal structure of the mouse Necl-4 full ectodomain and the structure of the heterophilic Necl ectodomain complex formed by the mNecl-4 and mNecl-1 ectodomains. We demonstrate that, while the ectodomain of mNecl-4 is monomeric, it forms a stable heterodimer with Ig1 of mNecl-1, with an affinity significantly higher than that observed for self-dimerization of the mNecl-1 ectodomain. We validated our structural characterizations by performing a surface plas

SUBMITTER: Liu X 

PROVIDER: S-EPMC6369812 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature