Literature DB >> 22221265

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

Melissa Love1, Jamie L Sandberg, Joshua J Ziarek, Kyle P Gerarden, Renee R Rode, Davin R Jensen, Darrell R McCaslin, Francis C Peterson, Christopher T Veldkamp.   

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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Year:  2012        PMID： 22221265      PMCID： PMC3272885          DOI： 10.1021/bi201601k

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


  28 in total

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  23 in total

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