5F4L

HIV-1 gp120 complex with JP-III-048

Summary for 5F4L

• Entry DOI: 10.2210/pdb5f4l/pdb
• Related: 5F4P 5F4R 5F4U
• Descriptor: ENVELOPE GLYCOPROTEIN GP120 of HIV-1 clade C, ~{N}'-[(1~{R},2~{R})-2-(carbamimidamidomethyl)-6-(methylaminomethyl)-2,3-dihydro-1~{H}-inden-1-yl]-~{N}-(4-chloranyl-3-fluoranyl-phenyl)ethanediamide (3 entities in total)
• Functional Keywords: crystal structure of hiv-1 gp120 complex with jp-iii-048, viral protein
• Biological source: Human immunodeficiency virus 1
• Total number of polymer chains: 2
• Total formula weight: 78486.87

Authors

Liang, S.,Hendrickson, W.A. (deposition date: 2015-12-03, release date: 2016-03-30, Last modification date: 2024-10-09)

Primary citation

Melillo, B.,Liang, S.,Park, J.,Schon, A.,Courter, J.R.,LaLonde, J.M.,Wendler, D.J.,Princiotto, A.M.,Seaman, M.S.,Freire, E.,Sodroski, J.,Madani, N.,Hendrickson, W.A.,Smith, A.B.
Small-Molecule CD4-Mimics: Structure-Based Optimization of HIV-1 Entry Inhibition.
Acs Med.Chem.Lett., 7:330-334, 2016

PubMed Abstract: The optimization, based on computational, thermodynamic, and crystallographic data, of a series of small-molecule ligands of the Phe43 cavity of the envelope glycoprotein gp120 of human immunodeficiency virus (HIV) has been achieved. Importantly, biological evaluation revealed that the small-molecule CD4 mimics (4-7) inhibit HIV-1 entry into target cells with both significantly higher potency and neutralization breadth than previous congeners, while maintaining high selectivity for the target virus. Their binding mode was characterized via thermodynamic and crystallographic studies.

PubMed: 26985324
DOI: 10.1021/acsmedchemlett.5b00471

Experimental method

X-RAY DIFFRACTION (2.7 Å)