Custom-made 15N-enriched CCL21 protein supplied by Protein Foundry
The chemokine CCL21 guides both T cell and metastatic cancer homing to lymph nodes by activating the receptor CCR7. CCL21 is among a handful of chemokines with an unstructured C-terminal extension. In a study published in Biochemistry, Yu Chen and colleagues at USF determined the crystal structure of a truncated CCL21 (residues 1–79) and monitored sulfotyrosine binding by 2D NMR. Their results reveal druggable hot spots resulting from an alternative N-loop conformation compared to the previously determined NMR structure of full-length CCL21. They also suggest a potential mechanism for the CCL21 autoinhibition that was discovered by Michael Sixt and coworkers.
Protein Foundry’s custom chemokine production and isotope labeling capabilities enabled the NMR binding studies described by Smith et al. Visit proteinfoundry.com to learn more about our full line of native, tagged, and custom-produced chemokine proteins.
2D NMR of 15N CCL21. NMR was used to monitor sulfotyrosine-induced chemical shift perturbations to CCL21 and identify a potential binding hot spot for this post-translational modification in the N-terminal extracellular domain of CCR7.
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