Langya virus (LayV) is a recently discovered henipavirus (HNV), isolated from febrile patients in China, harboring a genome distantly related to that of Nipah virus (NiV) and Hendra virus (HeV). HNV entry into host cells is mediated by the attachment (G) and fusion (F) glycoproteins which are the main targets of neutralizing antibodies. We show here that the LayV F and G glycoproteins promote membrane fusion with human, mouse and hamster target cells using a different, yet unknown, receptor than NiV and HeV and that NiV- and HeV-elicited monoclonal and polyclonal antibodies do not cross-react with LayV F and G. We determined cryo-electron microscopy structures of LayV F, in the prefusion and postfusion states, and of LayV G, revealing previously unknown conformational landscapes and explaining their distinct antigenicity relative to NiV and HeV. We computationally designed stabilized LayV G constructs and demonstrate the generalizability of an HNV F prefusion-stabilization strategy which will expedite vaccine development efforts. Our data will support the development of vaccines and therapeutics against LayV and closely related HNVs, such as the monoclonal antibodies characterized here.