Solution Structure of CCL21 and Identification of a Putative CCR7 Binding Site
| Autor: | Joshua J. Ziarek, Francis C. Peterson, Kyle P. Gerarden, Melissa Love, Renee R. Rode, Darrell R. McCaslin, Davin R. Jensen, Jamie L. Sandberg, Christopher T. Veldkamp |
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| Rok vydání: | 2012 |
| Předmět: |
Receptors
CCR7 endocrine system Chemokine Binding Sites Chemokine CCL21 biology CCR3 C-C chemokine receptor type 7 Plasma protein binding Crystallography X-Ray Biochemistry Molecular biology Article Protein Structure Tertiary Cell biology Chemokine receptor biology.protein Humans Binding site Nuclear Magnetic Resonance Biomolecular Conserved Sequence CCL22 Protein Binding CCL21 |
| Zdroj: | Biochemistry. 51:733-735 |
| ISSN: | 1520-4995 0006-2960 |
| Popis: | CCL21 is a human chemokine that recruits normal immune cells and metastasizing tumor cells to lymph nodes through activation of the G protein-coupled receptor CCR7. The CCL21 structure solved by NMR contains a conserved chemokine domain followed by an extended, unstructured C-terminus that is not typical of most other chemokines. A sedimentation equilibrium study showed CCL21 to be monomeric. Chemical shift mapping indicates that the CCR7 N-terminus binds to the N-loop and third β-strand of CCL21’s chemokine domain. Details of CCL21-receptor recognition may enable structure-based drug discovery of novel anti-metastatic agents. |
| Databáze: | OpenAIRE |
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