[HTML][HTML] The 1.5 Å crystal structure of human receptor for advanced glycation endproducts (RAGE) ectodomains reveals unique features determining ligand binding
HJ Park, JC Boyington - Journal of Biological Chemistry, 2010 - ASBMB
Interaction of the pattern recognition receptor, RAGE with key ligands such as advanced
glycation end products (AGE), S100 proteins, amyloid β, and HMGB1 has been linked to
diabetic complications, inflammatory and neurodegenerative disorders, and cancer. To help
answer the question of how a single receptor can recognize and respond to a diverse set of
ligands we have investigated the structure and binding properties of the first two
extracellular domains of human RAGE, which are implicated in various ligand binding and …
glycation end products (AGE), S100 proteins, amyloid β, and HMGB1 has been linked to
diabetic complications, inflammatory and neurodegenerative disorders, and cancer. To help
answer the question of how a single receptor can recognize and respond to a diverse set of
ligands we have investigated the structure and binding properties of the first two
extracellular domains of human RAGE, which are implicated in various ligand binding and …