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Related Concept Videos

Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
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Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
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Specificity for a CCR5 Inhibitor Is Conferred by a Single Amino Acid Residue: ROLE OF ILE198.

Gloria Lau1, Jean Labrecque1, Markus Metz2

  • 1From Anormed Inc., Langley, British Columbia V2Y 1N5, Canada.

The Journal of Biological Chemistry
|March 14, 2015
PubMed
Summary

Researchers identified a specific amino acid sequence in the CCR5 receptor responsible for the specificity of the CCR5 antagonist SCH-C. This finding aids in understanding HIV co-receptor binding and developing new inhibitors.

Keywords:
CC Chemokine Receptor Type 2b (CCR2b)CC Chemokine Receptor Type 5 (CCR5)Drug DesignHuman Immunodeficiency Virus (HIV)Molecular ModelingSite-directed Mutagenesis

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Area of Science:

  • Molecular Biology
  • Immunology
  • Virology

Background:

  • Chemokine receptors CCR5 and CCR2b exhibit high amino acid homology (89%).
  • CCR5 serves as a co-receptor for HIV entry, making CCR5 antagonists potential HIV inhibitors.
  • Understanding CCR5 antagonist binding is crucial for developing effective HIV therapies.

Purpose of the Study:

  • To probe the CCR5 inhibitor binding site using CCR5/CCR2b chimeric receptors.
  • To identify the specific amino acid sequences responsible for CCR5 antagonist specificity.

Main Methods:

  • Utilized CCR5/CCR2b chimeric receptors to assess compound inhibition.
  • Measured inhibition of chemokine-induced calcium flux using CCR5 antagonists SCH-C and TAK-779.
  • Performed sequence comparisons and targeted amino acid substitutions in chimeric receptors.

Main Results:

  • SCH-C specifically inhibited RANTES (CCL5)-mediated flux on CCR5 but not MCP-1 (CCL2)-mediated flux on CCR2b.
  • A CCR5/CCR2b chimera with CCR5 transmembrane domains IV-VI showed SCH-C inhibition of CCL2-induced flux.
  • Transferring a specific CCR5 sequence (KNFQTLKIV) into CCR2b conferred SCH-C inhibition; a single substitution (R206I) partially conferred inhibition.

Conclusions:

  • A limited amino acid sequence at the junction of transmembrane domain V and the second extracellular loop dictates SCH-C specificity for CCR5.
  • Proposed a model for SCH-C interaction with CCR5, involving residue Ile(198).
  • Findings provide insights into CCR5 antagonist binding mechanisms and potential for targeted drug design.