6onf

Crystal structure of HIV-1 LM/HT Clade A/E CRF01 gp120 core in complex with (S)-MCG-III-188-A02.

spinqualitylabelsall models 6onf, resolution 1.84Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6onf is a 1 chain structure with sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.842Å Ligands: EPE, MW4, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0M3KKW9_9HIV1 Publication Abstract from PubMed The HIV-1 envelope glycoprotein (Env) trimer mediates virus entry into cells. The "closed" conformation of Env is resistant to non-neutralizing antibodies (nnAbs). These antibodies mostly recognize occluded epitopes that can be exposed upon binding of CD4 or small-molecule CD4 mimetics (CD4mc). Here, we describe a new family of small molecules that expose Env to nnAbs and sensitize infected cells to antibody-dependent cellular cytotoxicity (ADCC). These compounds have limited capacity to inhibit virus infection directly, but are able to sensitize viral particles to neutralization by otherwise non-neutralizing antibodies. Structural analysis shows that some analogs of this family of CD4mc engage the gp120 Phe43 cavity by contacting the highly-conserved D368 residue, making them attractive scaffolds for drug development.IMPORTANCE HIV-1 has evolved multiple strategies to avoid humoral responses. One efficient mechanism is to keep its envelope glycoproteins (Env) in its "closed" conformation. Here we report on a new family of small molecules able to "open-up" Env, thus exposing vulnerable epitopes. This new family of molecules bind in the Phe43 cavity and contact the highly-conserved D368 residue. The structural and biological attributes of this family of molecules make them good candidates for drug development. A new family of small-molecule CD4-mimetic compounds contact the highly conserved aspartic acid 368 of HIV-1 gp120 and mediates ADCC.,Ding S, Grenier MC, Tolbert WD, Vezina D, Sherburn R, Richard J, Prevost J, Chapleau JP, Gendron-Lepage G, Medjahed H, Abrams C, Sodroski J, Pazgier M, Smith AB 3rd, Finzi A J Virol. 2019 Sep 25. pii: JVI.01325-19. doi: 10.1128/JVI.01325-19. PMID:31554684 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Gp120 3D structures

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