Reconstruction of a helical trimer by the second transmembrane domain of human copper transporter 2 in micelles and the binding of the trimer to silver

RSC Advances ◽  
2016 ◽  
Vol 6 (6) ◽  
pp. 4335-4342 ◽  
Author(s):  
Zhe Dong ◽  
Liping Guan ◽  
Chunyu Wang ◽  
Haoran Xu ◽  
Zhengqiang Li ◽  
...  

The second transmembrane domain of human copper transporter 2 (hCtr2-TMD2) forms a trimer with a weaker intermolecular interaction and a lower affinity for Ag(I) than hCtr1-TMD2 trimer.

2006 ◽  
Vol 26 (15) ◽  
pp. 5838-5849 ◽  
Author(s):  
Richard A. Colvin ◽  
Gabriele S. V. Campanella ◽  
Lindsay A. Manice ◽  
Andrew D. Luster

ABSTRACT CXCR3 is a G-protein-coupled seven-transmembrane domain chemokine receptor that plays an important role in effector T-cell and NK cell trafficking. Three gamma interferon-inducible chemokines activate CXCR3: CXCL9 (Mig), CXCL10 (IP-10), and CXCL11 (I-TAC). Here, we identify extracellular domains of CXCR3 that are required for ligand binding and activation. We found that CXCR3 is sulfated on its N terminus and that sulfation is required for binding and activation by all three ligands. We also found that the proximal 16 amino acid residues of the N terminus are required for CXCL10 and CXCL11 binding and activation but not CXCL9 activation. In addition, we found that residue R216 in the second extracellular loop is required for CXCR3-mediated chemotaxis and calcium mobilization but is not required for ligand binding or ligand-induced CXCR3 internalization. Finally, charged residues in the extracellular loops contribute to the receptor-ligand interaction. These findings demonstrate that chemokine activation of CXCR3 involves both high-affinity ligand-binding interactions with negatively charged residues in the extracellular domains of CXCR3 and a lower-affinity receptor-activating interaction in the second extracellular loop. This lower-affinity interaction is necessary to induce chemotaxis but not ligand-induced CXCR3 internalization, further suggesting that different domains of CXCR3 mediate distinct functions.


Metallomics ◽  
2014 ◽  
Vol 6 (3) ◽  
pp. 654 ◽  
Author(s):  
Carlos P. Huang ◽  
Mariama Fofana ◽  
Jefferson Chan ◽  
Christopher J. Chang ◽  
Stephen B. Howell

Metallomics ◽  
2015 ◽  
Vol 7 (11) ◽  
pp. 1477-1487 ◽  
Author(s):  
Cheng-Yu Tsai ◽  
Janika K. Liebig ◽  
Igor F. Tsigelny ◽  
Stephen B. Howell

We describe for the first time that the copper transporter 1 (CTR1) is important to maintain the stability of copper transporter 2 (CTR2).


2010 ◽  
Vol 79 (1) ◽  
pp. 157-166 ◽  
Author(s):  
Brian G. Blair ◽  
Christopher A. Larson ◽  
Preston L. Adams ◽  
Paolo B. Abada ◽  
Catherine E. Pesce ◽  
...  

2010 ◽  
Vol 11 (11) ◽  
pp. 4741-4749 ◽  
Author(s):  
Jesse Bertinato ◽  
Sébastien Duval ◽  
Mary R. L’Abbé

2010 ◽  
Vol 78 (3) ◽  
pp. 333-339 ◽  
Author(s):  
Christopher A. Larson ◽  
Preston L. Adams ◽  
Brian G. Blair ◽  
Roohangiz Safaei ◽  
Stephen B. Howell

2010 ◽  
Vol 77 (6) ◽  
pp. 912-921 ◽  
Author(s):  
Brian G. Blair ◽  
Christopher A. Larson ◽  
Preston L. Adams ◽  
Paolo B. Abada ◽  
Roohangiz Safaei ◽  
...  

2009 ◽  
Vol 15 (13) ◽  
pp. 4312-4321 ◽  
Author(s):  
Brian G. Blair ◽  
Christopher A. Larson ◽  
Roohangiz Safaei ◽  
Stephen B. Howell

Sign in / Sign up

Export Citation Format

Share Document