Structural basis of coreceptor recognition by HIV-1 envelope spike.

ABSTRACT: HIV-1 envelope glycoprotein (Env), which consists of trimeric (gp160)₃ cleaved to (gp120 and gp41)₃, interacts with the primary receptor CD4 and a coreceptor (such as chemokine receptor CCR5) to fuse viral and target-cell membranes. The gp120-coreceptor interaction has previously been proposed as the most crucial trigger for unleashing the fusogenic potential of gp41. Here we report a cryo-electron microscopy structure of a full-length gp120 in complex with soluble CD4 and unmodified human CCR5, at 3.9 Å resolution. The V3 loop of gp120 inserts into the chemokine-binding pocket formed by seven transmembrane helices of CCR5, and the N terminus of CCR5 contacts the CD4-induced bridging sheet of gp120. CCR5 induces no obvious allosteric changes in gp120 that can propagat

SUBMITTER: Shaik MM 

PROVIDER: S-EPMC6391877 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature