Stoichiometry of LTbetaR binding to LIGHT

LTbetaR is a member of the TNF receptor family of proteins. It binds to two different cell surface ligands, LIGHT, a homotypic trimer, and LTalpha1beta2, a heterotypic trimer. We have measured the affinities of the dimeric IgG fusion protein, LTbetaRIgG, and monomeric LTbetaR protein binding to both...

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Bibliographic Details
Published in:Biochemistry (Easton) 2006-08, Vol.45 (33), p.10117-10128
Main Authors: Eldredge, John, Berkowitz, Steven, Corin, Alan F, Day, Eric S, Hayes, David, Meier, Werner, Strauch, Kathy, Zafari, Mohammad, Tadi, Madhavi, Farrington, Graham K
Format: Article
Language:English
Subjects:
Binding Sites
Calorimetry - methods
Cell Physiological Phenomena
Chromatography, Gel
Dimerization
Electrophoresis, Polyacrylamide Gel
Immunoglobulin G - metabolism
Ligands
Lymphotoxin-alpha - chemistry
Lymphotoxin-alpha - metabolism
Models, Molecular
Molecular Weight
Receptors, Tumor Necrosis Factor - chemistry
Receptors, Tumor Necrosis Factor - metabolism
Recombinant Fusion Proteins - metabolism
Surface Plasmon Resonance
Thermodynamics
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Summary:LTbetaR is a member of the TNF receptor family of proteins. It binds to two different cell surface ligands, LIGHT, a homotypic trimer, and LTalpha1beta2, a heterotypic trimer. We have measured the affinities of the dimeric IgG fusion protein, LTbetaRIgG, and monomeric LTbetaR protein binding to both LIGHT and LTalpha1beta2 using surface plasmon resonance and found values of
ISSN:0006-2960