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

Biochemistry. 2012 Jan 24;51(3):733-5. doi: 10.1021/bi201601k. Epub 2012 Jan 17.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Binding Sites
  • Chemokine CCL21 / chemistry*
  • Chemokine CCL21 / metabolism*
  • Conserved Sequence
  • Crystallography, X-Ray
  • Humans
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Binding
  • Protein Structure, Tertiary
  • Receptors, CCR7 / chemistry*
  • Receptors, CCR7 / metabolism*


  • CCR7 protein, human
  • Chemokine CCL21
  • Receptors, CCR7

Associated data

  • PDB/17245
  • PDB/2L4N