ArticleBiochemistry2016
Crystallographic Structure of Truncated CCL21 and the Putative Sulfotyrosine-Binding Site.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- C-C Chemokine Receptor 7 Promotes T-Cell Acute Lymphoblastic Leukemia Invasion of the Central Nervous System via β2-Integrins.International journal of molecular sciences · 2024Article
- NMR indicates the N-termini of PSGL1 and CCR7 bind competitively to the chemokine CCL21.Biochemistry and biophysics reports · 2023Article
- Fragment-based drug discovery of small molecule ligands for the human chemokine CCL28.SLAS discovery : advancing life sciences R & D · 2023Article
- Structural Insights into Molecular Recognition by Human Chemokine CCL19.Biochemistry · 2022Article
- The non-ELR CXC chemokine encoded by human cytomegalovirus UL146 genotype 5 contains a C-terminal β-hairpin and induces neutrophil migration as a selective CXCR2 agonist.PLoS pathogens · 2022Article
- A highly efficient method for the production and purification of recombinant human CXCL8.PloS one · 2021Article
- Structural Features of an Extended C-Terminal Tail Modulate the Function of the Chemokine CCL21.Biochemistry · 2020Article
- Differences in Sulfotyrosine Binding amongst CXCR1 and CXCR2 Chemokine Ligands.International journal of molecular sciences · 2017Article
- CCR7 Sulfotyrosine Enhances CCL21 Binding.International journal of molecular sciences · 2017Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
CCL21 chemokine binds the G protein-coupled receptor CCR7, aiding not only in immune response but also in cancer metastasis. Compared with other chemokines, CCL21 has a unique extended unstructured C-terminus that is truncated in some naturally occurring variants. We have determined the X-ray crystallographic structure of a truncated CCL21 (residues 1-79) lacking the extended C-terminus and identified, via two-dimensional nuclear magnetic resonance (NMR), a putative sulfotyrosine-binding site that may recognize such post-translationally modified tyrosine residues on the receptor. Compared to the previously determined NMR structure of full-length CCL21, the crystal structure presents new druggable binding hot spots resulting from an alternative N-loop conformation. In addition, whereas the previous NMR structure did not provide any structural information after residue 70, the C-terminus of the truncated CCL21, ordered up to Ala77 in our crystal structure, is placed near the N-loop and sulfotyrosine-binding site, indicating that the extended C-terminus of full-length CCL21 can interact with this important region for receptor binding. These observations suggest a potential origin for the autoinhibition of CCL21 activity that was recently described. The new crystal structure and binding hot spot analysis have important implications for the function of the CCL21 C-terminus and drug discovery.
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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.