ArticleInternational journal of molecular sciences2011
Sulfotyrosine recognition as marker for druggable sites in the extracellular space.
Article in International journal of molecular sciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- Specific residues and conformational plasticity define the substrate specificity of short-chain dehydrogenases/reductases.The Journal of biological chemistry · 2024Article
- Fragment-based drug discovery of small molecule ligands for the human chemokine CCL28.SLAS discovery : advancing life sciences R & D · 2023Article
- The binding and specificity of chemokine binding proteins, through the lens of experiment and computation.Biomedical journal · 2022Review
- Protein engineering of the chemokine CCL20 prevents psoriasiform dermatitis in an IL-23-dependent murine model.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Differences in Sulfotyrosine Binding amongst CXCR1 and CXCR2 Chemokine Ligands.International journal of molecular sciences · 2017Article
- Exploiting agonist biased signaling of chemokines to target cancer.Molecular carcinogenesis · 2017Article
- Crystallographic Structure of Truncated CCL21 and the Putative Sulfotyrosine-Binding Site.Biochemistry · 2016Article
- Structural analysis of a novel small molecule ligand bound to the CXCL12 chemokine.Journal of medicinal chemistry · 2014Article
- The structural role of receptor tyrosine sulfation in chemokine recognition.British journal of pharmacology · 2014Review
- Sulfopeptide probes of the CXCR4/CXCL12 interface reveal oligomer-specific contacts and chemokine allostery.ACS chemical biology · 2013Article
- NMR in the Analysis of Functional Chemokine Interactions and Drug Discovery.Drug discovery today. Technologies · 2012Article
- Fragment-based optimization of small molecule CXCL12 inhibitors for antagonizing the CXCL12/CXCR4 interaction.Current topics in medicinal chemistry · 2012Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Chemokine signaling is a well-known agent of autoimmune disease, HIV infection, and cancer. Drug discovery efforts for these signaling molecules have focused on developing inhibitors targeting their associated G protein-coupled receptors. Recently, we used a structure-based approach directed at the sulfotyrosine-binding pocket of the chemokine CXCL12, and thereby demonstrated that small molecule inhibitors acting upon the chemokine ligand form an alternative therapeutic avenue. Although the 50 members of the chemokine family share varying degrees of sequence homology (some as little as 20%), all members retain the canonical chemokine fold. Here we show that an equivalent sulfotyrosine-binding pocket appears to be conserved across the chemokine superfamily. We monitored sulfotyrosine binding to four representative chemokines by NMR. The results suggest that most chemokines harbor a sulfotyrosine recognition site analogous to the cleft on CXCL12 that binds sulfotyrosine 21 of the receptor CXCR4. Rational drug discovery efforts targeting these sites may be useful in the development of specific as well as broad-spectrum chemokine inhibitors.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.