The extracellular region of the receptor for advanced glycation end products is composed of two independent structural units.

ABSTRACT: 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 small approximately 40 residue cytosolic domain and a large extracellular region composed of 3 Ig-like domains. In this study, high level bacterial expression systems and purification protocols were generated for the extracellular region of RAGE (sRAGE) and the five permutations of single and tandem domain constructs to enable biophysical and structural characterization of its tertiary and quaternary structure. The structure and stability of each of these six protein constructs was assayed by b

SUBMITTER: Dattilo BM 

PROVIDER: S-EPMC2527459 | biostudies-literature | 2007 Jun

REPOSITORIES: biostudies-literature