Solution structure of CCL21 and identification of a putative CCR7 binding site |
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| Authors: | Love Melissa Sandberg Jamie L Ziarek Joshua J Gerarden Kyle P Rode Renee R Jensen Davin R McCaslin Darrell R Peterson Francis C Veldkamp Christopher T |
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| Affiliation: | Department of Chemistry, University of Wisconsin-Whitewater, Whitewater, Wisconsin 53190, United States. |
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| Abstract: | 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 antimetastatic agents. |
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