2MOV: Receptor for Advanced Glycation End Products (RAGE) Specifically Recognizes Methylglyoxal Derived AGEs

Citation:
Abstract
Diabetes-induced hyperglycemia increases the extracellular concentration of methylglyoxal. Methylglyoxal-derived hydroimidazolones (MG-H) form advanced glycation end products (AGEs) that accumulate in the serum of diabetic patients. The binding of hydroimidozolones to the receptor for AGEs (RAGE) results in long-term complications of diabetes typified by vascular and neuronal injury. Here we show that binding of methylglyoxal-modified albumin to RAGE results in signal transduction. Chemically synthesized peptides containing hydroimidozolones bind specifically to the V domain of RAGE with nanomolar affinity. The solution structure of an MG-H1-V domain complex revealed that the hydroimidazolone moiety forms multiple contacts with a positively charged surface on the V domain. The high affinity and specificity of hydroimidozolones binding to the V domain of RAGE suggest that they are the primary AGE structures that give rise to AGEs-RAGE pathologies.
PDB ID: 2MOVDownload
MMDB ID: 120918
PDB Deposition Date: 2014/5/5
Updated in MMDB: 2014/06
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2MOV: monomeric; determined by author
Molecular Components in 2MOV
Label Count Molecule
Protein (1 molecule)
1
Advanced Glycosylation END Product-specific Receptor(Gene symbol: AGER)
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

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