RANKL Employs Distinct Binding Modes to Engage RANK and the Osteoprotegerin Decoy Receptor期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

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RANKL Employs Distinct Binding Modes to Engage RANK and the Osteoprotegerin Decoy Receptor

Authors:	Christopher A Nelson Julia T Warren Michael W-H Wang Steven L Teitelbaum Daved H Fremont

Institution:	1. Department of Pathology and Immunology, Washington University School of Medicine, 660 S. Euclid Avenue, St. Louis, MO 63110-1093, USA;2. Department of Internal Medicine, Washington University School of Medicine, 660 S. Euclid Avenue, St. Louis, MO 63110-1093, USA;3. Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 S. Euclid Avenue, St. Louis, MO 63110-1093, USA

Abstract:	Download : Download high-res image (257KB) Download : Download full-size image Highlights? Crystal structures of the cytokine-binding regions of OPG and RANK bound to RANKL ? High-affinity OPG engagement is associated with a distinct RANKL-binding cleft ? Structural basis of how the OPG^F96L mutation promotes juvenile Paget’s disease

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