The Extracellular Region of the Receptor for Advanced Glycation End Products Is Composed of Two Independent Structural Units

• Published in: Biochemistry (Easton) Vol. 46; no. 23; pp. 6957 - 6970
• Main Authors: Dattilo, Brian M, Fritz, Günter, Leclerc, Estelle, Vander Kooi, Craig W, Heizmann, Claus W, Chazin, Walter J
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 12.06.2007
• Subjects: Amino Acid Sequence; Base Sequence; Cloning, Molecular; DNA - chemistry; DNA - genetics; Escherichia coli - genetics; Glycation End Products, Advanced - chemistry; Glycation End Products, Advanced - metabolism; Humans; Models, Molecular; Molecular Sequence Data; Peptide Fragments - chemistry; Protein Conformation; Receptor for Advanced Glycation End Products; Receptors, Immunologic - chemistry; Receptors, Immunologic - genetics; Receptors, Immunologic - metabolism; Recombinant Proteins - chemistry; Recombinant Proteins - metabolism

The receptor for advanced glycation end products (RAGE) is an important cell surface receptor being pursued as a therapeutic target because it has been implicated in complications arising from diabetes and chronic inflammatory conditions. RAGE is a single membrane spanning receptor containing a very...