ArticleJournal of molecular biology2011
The conformation and orientation of a 27-residue CCR5 peptide in a ternary complex with HIV-1 gp120 and a CD4-mimic peptide.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 42 citations in OpenAlex.
- Distinct genetic clusters in HIV-1 CRF01_AE-infected patients induced variable degrees of CD4mBio · 2024Article
- Platelets in HIV: A Guardian of Host Defence or Transient Reservoir of the Virus?Frontiers in immunology · 2021Review
- Defining rules governing recognition and Fc-mediated effector functions to the HIV-1 co-receptor binding site.BMC biology · 2020Article
- Mapping Interaction Sites on Human Chemokine Receptors by Deep Mutational Scanning.Journal of immunology (Baltimore, Md. : 1950) · 2018Article
- The solution structure of monomeric CCL5 in complex with a doubly sulfated N-terminal segment of CCR5.The FEBS journal · 2018Article
- Design of HIV Coreceptor Derived Peptides That Inhibit Viral Entry at Submicromolar Concentrations.Molecular pharmaceutics · 2017Article
- Design and synthesis of small molecule-sulfotyrosine mimetics that inhibit HIV-1 entry.Bioorganic & medicinal chemistry · 2016Article
- Incompatible Natures of the HIV-1 Envelope in Resistance to the CCR5 Antagonist Cenicriviroc and to Neutralizing Antibodies.Antimicrobial agents and chemotherapy · 2016Article
- The C4 region as a target for HIV entry inhibitors--NMR mapping of the interacting segments of T20 and gp120.The FEBS journal · 2015Article
- An extended CCR5 ECL2 peptide forms a helix that binds HIV-1 gp120 through non-specific hydrophobic interactions.The FEBS journal · 2015Article
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- Coevolution Analysis of HIV-1 Envelope Glycoprotein Complex.PloS one · 2015Article
- Functional Mimetics of the HIV-1 CCR5 Co-Receptor Displayed on the Surface of Magnetic Liposomes.PloS one · 2015Article
- topPTM: a new module of dbPTM for identifying functional post-translational modifications in transmembrane proteins.Nucleic acids research · 2014Article
- Article
- Molecular recognition of CCR5 by an HIV-1 gp120 V3 loop.PloS one · 2014Article
- Modelling binding between CCR5 and CXCR4 receptors and their ligands suggests the surface electrostatic potential of the co-receptor to be a key player in the HIV-1 tropism.Retrovirology · 2013Article
- Linking genotype to phenotype on beads: high throughput selection of peptides with biological function.Scientific reports · 2013Article
- NMR mapping of RANTES surfaces interacting with CCR5 using linked extracellular domains.The FEBS journal · 2013Article
Corrections and comments
- Erratum issued
Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
Abstract
Interaction of CC chemokine receptor 5 (CCR5) with the human immunodeficiency virus type 1 (HIV-1) gp120/CD4 complex involves its amino-terminal domain (Nt-CCR5) and requires sulfation of two to four tyrosine residues in Nt-CCR5. The conformation of a 27-residue Nt-CCR5 peptide, sulfated at Y10 and Y14, was studied both in its free form and in a ternary complex with deglycosylated gp120 and a CD4-mimic peptide. NMR experiments revealed a helical conformation at the center of Nt-CCR5(1-27), which is induced upon gp120 binding, as well as a helical propensity for the free peptide. A well-defined structure for the bound peptide was determined for residues 7-23, increasing by 2-fold the length of Nt-CCR5's known structure. Two-dimensional saturation transfer experiments and measurement of relaxation times highlighted Nt-CCR5 residues Y3, V5, P8-T16, E18, I23 and possibly D2 as the main binding determinant. A calculated docking model for Nt-CCR5(1-27) suggests that residues 2-22 of Nt-CCR5 interact with the bases of V3 and C4, while the C-terminal segment of Nt-CCR5(1-27) points toward the target cell membrane, reflecting an Nt-CCR5 orientation that differs by 180° from that of a previous model. A gp120 site that could accommodate (CCR5)Y3 in a sulfated form has been identified. The present model attributes a structural basis for binding interactions to all gp120 residues previously implicated in Nt-CCR5 binding. Moreover, the strong interaction of sulfated (CCR5)Tyr14 with (gp120)Arg440 revealed by the model and the previously found correlation between E322 and R440 mutations shed light on the role of these residues in HIV-1 phenotype conversion, furthering our understanding of CCR5 recognition by HIV-1.
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