NMR mapping of RANTES surfaces interacting with CCR5 using linked extracellular domains (pages 2068–2084)
Einat Schnur, Naama Kessler, Yuri Zherdev, Eran Noah, Tali Scherf, Fa-Xiang Ding, Svetlana Rabinovich, Boris Arshava, Victoria Kurbatska, Ainars Leonciks, Alexander Tsimanis, Osnat Rosen, Fred Naider and Jacob Anglister
Version of Record online: 2 APR 2013 | DOI: 10.1111/febs.12230
CCR5 extracellular domains were linked by either biosynthesis in Escherichia coli or by chemical synthesis to overcome the low affinity of ECL peptides to the receptors. Using these chimeras, Nt-CCR5 and ECL2 were found to be the major contributors to CCR5 binding to RANTES, creating a nearly closed ring around this protein by interacting with opposing faces of the chemokine.