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NMR mapping of RANTES surfaces interacting with CCR5 using linked extracellular domains
Einat Schnur1, Naama Kessler, Yuri Zherdev
1Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
The FEBS Journal
|March 14, 2013
Summary
Chemokine receptor extracellular domains were linked to study binding to chemokines. The N-terminal peptide and extracellular loop 2 of CC chemokine receptor 5 (CCR5) are key for binding RANTES.
Area of Science:
- Molecular biology
- Immunology
- Biochemistry
Background:
- Chemokines are small proteins regulating leukocyte trafficking.
- They bind G-protein-coupled receptors (GPCRs).
- Interactions between chemokine receptors' extracellular loops and chemokines are poorly understood due to low peptide affinities.
Purpose of the Study:
- To investigate the interactions between CC chemokine receptor 5 (CCR5) extracellular domains and the chemokine RANTES.
- To overcome the low affinity of extracellular loop (ECL) peptides to chemokines.
Main Methods:
- Linked two or three CCR5 extracellular domains via biosynthesis or chemical synthesis.
- Used (1H-15N-HSQC) spectra to monitor RANTES binding to CCR5 peptides.
- Analyzed the structural similarities between RANTES-CCR5 interactions and HIV-1 gp120.
Main Results:
- N-terminal (Nt-) CCR5 and ECL2 were identified as major contributors to RANTES binding.
- These domains form a ring-like structure around RANTES.
- Identified similarities between RANTES binding surfaces and HIV-1 gp120 surfaces.
Conclusions:
- The study provides insights into chemokine-chemokine receptor interactions.
- Developed novel methods for linking GPCR extracellular domains.
- These methods can be applied to study other chemokine receptor-ligand interactions.
