Solution structure, conformational dynamics, and CD4-induced activation in full-length, glycosylated, monomeric HIV gp120.

ABSTRACT: The gp120 subunit of the HIV Env glycoprotein is responsible for receptor interactions leading to viral entry and is a primary target for neutralizing antibodies. Most structural studies have focused on the heavily truncated, deglycosylated gp120 core, leaving fundamental aspects of the glycoprotein that are responsible for immune evasion and receptor-induced activation unresolved. Here we investigate full-length, glycosylated HIV gp120 in unliganded and CD4-bound forms by using small-angle X-ray scattering to visualize global structural reorganization and hydrogen/deuterium exchange to track changes in local conformational dynamics. The studies revealed unliganded full-length gp120 to be considerably more dynamic, particularly at the CD4 binding site, than suggested by previous studies of

SUBMITTER: Guttman M 

PROVIDER: S-EPMC3421722 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature