Conformational Variability of HIV-1 Env Trimer and Viral Vulnerability.

ABSTRACT: HIV-1 envelope glycoprotein (Env) is critical for viral fusion and entry into host cells and remains a primary target for vaccine and antiviral drug development. Advances in soluble gp140 trimer design have provided insight into the ectodomain structure and dynamics. However, the membrane-proximal external region (MPER) and transmembrane domain (TMD) are comparatively understudied, and knowledge of the cytoplasmic tail (CT) is virtually absent. Additionally, the ectodomain and TMD have been investigated separately in previous studies. To investigate the trimeric gp120-gp41 as a complete entity and its structural flexibility, we built a full-length model of the gp120-gp41 trimer that is fully glycosylated with N-linked glycans and embedded in a lipid bilayer, and performed all-atom molecula

SUBMITTER: Cao Y 

PROVIDER: S-EPMC12632500 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature