The affinity of human RANK binding to its ligand RANKL

• Published in: Archives of biochemistry and biophysics Vol. 487; no. 1; pp. 49 - 53
• Main Authors: Zhang, Shiqian, Liu, Changzhen, Huang, Peng, Zhou, Shu, Ren, Jingshan, Kitamura, Yoshihiro, Tang, Peifu, Bi, Zhenggang, Gao, Bin
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.07.2009
• Subjects: Affinity of RANK–RANKL; Base Sequence; Bone; Chromatography; Digestion; DNA Primers - genetics; Enzymes; Escherichia coli; Escherichia coli - genetics; Filtration; Fusion protein; Humans; Immune response; In Vitro Techniques; Inclusion bodies; Kinetics; Ligands; Mammary gland; Monomers; NF- Kappa B protein; Protein Interaction Domains and Motifs; Protein Structure, Tertiary; RANK ligand; RANK Ligand - chemistry; RANK Ligand - genetics; RANK Ligand - metabolism; RANK–RANKL interaction; Receptor activator of nuclear factor-kappa B; Receptor Activator of Nuclear Factor-kappa B - chemistry; Receptor Activator of Nuclear Factor-kappa B - genetics; Receptor Activator of Nuclear Factor-kappa B - metabolism; Receptor mechanisms; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Surface Plasmon Resonance; TRANCE protein; Vascular diseases; RANK–RANKL interaction; Affinity of RANK–RANKL; RANK ligand; Receptor activator of nuclear factor-kappa B; Surface plasmon resonance

Receptor activator of nuclear factor-kappa B (RANK) and its ligand, RANKL play critical roles in bone re-modeling, immune function, vascular disease and mammary gland development. To study the interaction of RANK and RANKL, we have expressed both extracellular domain of RANK and ectodomain of RANKL...