![ae pixel sorter 1.0.2 ae pixel sorter 1.0.2](http://datamoshing.com/wp-content/uploads/2016/06/pixel-sorted-1038x576.jpg)
Structure of CC chemokine receptor 5 with a potent chemokine antagonist reveals mechanisms of chemokine recognition and molecular mimicry by HIV. Molecular recognition of CCR5 by an HIV-1 gp120 V3 loop. Molecular recognition of CXCR4 by a dual tropic HIV-1 gp120 V3 loop. Structure of the CCR5 chemokine receptor-HIV entry inhibitor maraviroc complex. Cryo-EM structure of a CD4-bound open HIV-1 envelope trimer reveals structural rearrangements of the gp120 V1V2 loop. Structure and immune recognition of trimeric pre-fusion HIV-1 Env. Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer. Crystal structure of a soluble cleaved HIV-1 envelope trimer. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. These results advance our understanding of HIV-1 entry into host cells and may guide the development of vaccines and therapeutic agents. The coreceptor probably functions by stabilizing and anchoring the CD4-induced conformation of Env near the cell membrane.
![ae pixel sorter 1.0.2 ae pixel sorter 1.0.2](https://dls1.gfxplugin.ir/Download_Files/2247/SearchSmall/banner.jpg)
The N terminus of gp120, which is gripped by gp41 in the pre-fusion or CD4-bound Env, flips back in the CCR5-bound conformation and may irreversibly destabilize gp41 to initiate fusion. CCR5 induces no obvious allosteric changes in gp120 that can propagate to gp41 it does bring the Env trimer close to the target membrane. 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. 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 gp120–coreceptor interaction has previously been proposed as the most crucial trigger for unleashing the fusogenic potential of gp41. 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.