Structural basis of chemokine receptor function - A model for binding affinity and ligand selectivity

Lavanya Rajagopalan, Krishna Rajarathnam

Research output: Contribution to journalReview articlepeer-review

116 Scopus citations


Chemokine receptors play fundamental roles in human physiology from embryogenesis to inflammatory response. The receptors belong to the G-protein coupled receptor class, and are activated by chemokine ligands with a range of specificities and affinities that result in a complicated network of interactions. The molecular basis for function is largely a black box, and can be directly attributed to the lack of structural information on the receptors. Studies to date indicate that function can be best described by a two-site model, that involves interactions between the receptor N-domain and ligand N-terminal loop residues (site-I), and between receptor extracellular loop and the ligand N-terminal residues (site-II). In this review, we describe how the two-site model could modulate binding affinity and ligand selectivity, and also highlight some of the unique chemokine receptor features, and their role in function.

Original languageEnglish (US)
Pages (from-to)325-339
Number of pages15
JournalBioscience Reports
Issue number5
StatePublished - Oct 2006
Externally publishedYes


  • Binding affinity
  • Chemokine
  • Chemokine receptor
  • GPCR
  • N-terminal domain
  • Receptor activation structure-function
  • Selectivity

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology
  • Cell Biology


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