Sulfotyrosine Recognition as Marker for Druggable Sites in the Extracellular Space
Author Information
Author(s): Ziarek Joshua J., Heroux Maxime S., Veldkamp Christopher T., Peterson Francis C., Volkman Brian F.
Primary Institution: Medical College of Wisconsin
Hypothesis
A sulfotyrosine-binding pocket analogous to the sTyr21 recognition site on CXCL12 may be present across the entire human chemokine superfamily.
Conclusion
The study identifies a conserved sulfotyrosine binding site in the chemokine superfamily that could be targeted for drug discovery.
Supporting Evidence
- Chemokines are involved in various diseases, including autoimmune diseases and cancer.
- Small molecule inhibitors targeting chemokines may provide alternative therapeutic options.
- The study demonstrated that most chemokines have a sulfotyrosine recognition site similar to CXCL12.
Takeaway
Chemokines, which help cells move in the body, have a special spot that can grab onto a molecule called sulfotyrosine, and this spot is similar across many chemokines, making it a good target for new medicines.
Methodology
The study used NMR spectroscopy to monitor sulfotyrosine binding to various chemokines and performed multiple sequence alignments to identify conserved residues.
Limitations
The study could not model certain chemokines due to low sequence homology, and the binding interactions were primarily inferred from chemical shift perturbations.
Digital Object Identifier (DOI)
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