Solution structure of CCL21 and identification of a putative CCR7 binding site. Biochemistry 2012 Jan 24;51(3):733-5
Date
01/10/2012Pubmed ID
22221265Pubmed Central ID
PMC3272885DOI
10.1021/bi201601kScopus ID
2-s2.0-84856253909 (requires institutional sign-in at Scopus site) 40 CitationsAbstract
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.
Author List
Love M, Sandberg JL, Ziarek JJ, Gerarden KP, Rode RR, Jensen DR, McCaslin DR, Peterson FC, Veldkamp CTAuthor
Francis C. Peterson PhD Professor in the Biochemistry department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Binding SitesChemokine CCL21
Conserved Sequence
Crystallography, X-Ray
Humans
Nuclear Magnetic Resonance, Biomolecular
Protein Binding
Protein Structure, Tertiary
Receptors, CCR7