Biochemistry 2006, 45, 10117-10128
10117
Stoichiometry of LTβR Binding to LIGHT John Eldredge,‡ Steven Berkowitz,‡ Alan F. Corin,‡ Eric S. Day,‡ David Hayes,§ Werner Meier,‡ Kathy Strauch,‡ Mohammad Zafari,‡ Madhavi Tadi,‡ and Graham K. Farrington*,‡ Biogen Idec, Inc., 12 Cambridge Center, Cambridge, Massachusetts 02142, and Boston Biomedical Research Institute, 64 GroVe Street, Watertown, Massachusetts 02472 ReceiVed February 1, 2006; ReVised Manuscript ReceiVed June 7, 2006
ABSTRACT: LTβR is a member of the TNF receptor family of proteins. It binds to two different cell surface ligands, LIGHT, a homotypic trimer, and LTR1β2, a heterotypic trimer. We have measured the affinities of the dimeric IgG fusion protein, LTβRIgG, and monomeric LTβR protein binding to both LIGHT and LTR1β2 using surface plasmon resonance and found values of
