个性化文献订阅>期刊> Biochemistry
 

Solution Structure of CCL21 and Identification of a Putative CCR7 Binding Site

  作者 Love, M; Sandberg, JL; Ziarek, JJ; Gerarden, KP; Rode, RR; Jensen, DR; McCaslin, DR; Peterson, FC; Veldkamp, CT  
  选自 期刊  Biochemistry;  卷期  2012年51-3;  页码  733-735  
  关联知识点  
 

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

 
      被申请数(0)  
 

[全文传递流程]

一般上传文献全文的时限在1个工作日内