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Solution structure of CCL21 and identification of a putative CCR7 binding site.

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 ?-strand of CCL21's chemokine domain. Details of CCL21-receptor recognition may enable structure-based drug discovery of novel antimetastatic agents.

SUBMITTER: Love M

PROVIDER: S-EPMC3272885 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature

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Solution structure of CCL21 and identification of a putative CCR7 binding site.

Love Melissa M Sandberg Jamie L JL Ziarek Joshua J JJ Gerarden Kyle P KP Rode Renee R RR Jensen Davin R DR McCaslin Darrell R DR Peterson Francis C FC Veldkamp Christopher T CT

Biochemistry 20120117 3

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 CCL2 ...[more]

PMID: 22221265

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