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Structure of the CCR5 chemokine receptor-HIV entry inhibitor maraviroc complex

Academic Article
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Overview

authors

  • Tan, Q.
  • Zhu, Y.
  • Li, J.
  • Chen, Z.
  • Han, G. W.
  • Kufareva, I.
  • Li, T.
  • Ma, L.
  • Fenalti, G.
  • Li, J.
  • Zhang, W.
  • Xie, X.
  • Yang, H.
  • Jiang, H.
  • Cherezov, Vadim
  • Liu, H.
  • Stevens, Raymond
  • Zhao, Q.
  • Wu, B.

publication date

  • September 2013

journal

  • Science  Journal

abstract

  • The CCR5 chemokine receptor acts as a co-receptor for HIV-1 viral entry. Here we report the 2.7 angstrom-resolution crystal structure of human CCR5 bound to the marketed HIV drug maraviroc. The structure reveals a ligand-binding site that is distinct from the proposed major recognition sites for chemokines and the viral glycoprotein gp120, providing insights into the mechanism of allosteric inhibition of chemokine signaling and viral entry. A comparison between CCR5 and CXCR4 crystal structures, along with models of co-receptor-gp120-V3 complexes, suggests that different charge distributions and steric hindrances caused by residue substitutions may be major determinants of HIV-1 co-receptor selectivity. These high-resolution insights into CCR5 can enable structure-based drug discovery for the treatment of HIV-1 infection.

subject areas

  • Binding Sites
  • Cyclohexanes
  • HIV Envelope Protein gp120
  • HIV Fusion Inhibitors
  • HIV-1
  • Humans
  • Ligands
  • Protein Conformation
  • Receptors, CCR5
  • Receptors, CXCR4
  • Triazoles
  • Virus Internalization
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Identity

PubMed Central ID

  • PMC3819204

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1241475

PubMed ID

  • 24030490
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Additional Document Info

start page

  • 1387

end page

  • 1390

volume

  • 341

issue

  • 6152

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