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Advanced Glycation End Product Recognition by the Receptor for AGEs

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TLDR
The solution structure of a CEL-containing peptide-RAGE V domain complex reveals that the carboxyethyl moiety fits inside a positively charged cavity of the V domain.
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This article is published in Structure.The article was published on 2011-05-11 and is currently open access. It has received 186 citations till now. The article focuses on the topics: RAGE (receptor) & Glycation.

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Receptor for AGE (RAGE): signaling mechanisms in the pathogenesis of diabetes and its complications.

TL;DR: It is suggested that levels of soluble RAGEs and polymorphisms in the gene encoding RAGE may hold promise for the identification of patients who are vulnerable to the complications of diabetes and/or are receptive to therapeutic interventions designed to prevent and reverse the damage inflicted by chronic hyperglycemia, irrespective of its etiology.
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RAGE: a single receptor fits multiple ligands

TL;DR: A putative mechanism of RAGE ligand recognition of receptor activation is proposed and it is suggested that ligand binding is driven largely by electrostatic interactions between the positively charged surface of the ectodomain and negatively charged ligands.
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Role of advanced glycation end products in cardiovascular disease

TL;DR: The purpose of this review is to discuss the role of AGEs in cardiovascular disease and in particular in heart failure, focussing on both cellular mechanisms of action as well as highlighting how targeting A GEs may represent a novel therapeutic strategy in the treatment of HF.
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Vascular effects of advanced glycation endproducts: Clinical effects and molecular mechanisms.

TL;DR: The enhanced generation and accumulation of advanced glycation endproducts (AGEs) have been linked to increased risk for macrovascular and microvascular complications associated with diabetes mellitus, and understanding the pathogenic mechanisms of AGEs is paramount to develop strategies against diabetic and cardiovascular complications.
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Advanced glycation end products in the pathogenesis of chronic kidney disease.

TL;DR: The receptor for A GEs, RAGE, is important in development of CKD, but its interaction with AGEs in vivo remains enigmatic; other ligands and ternary complexation may be influential.
References
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Journal ArticleDOI

SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling.

Nicolas Guex, +1 more
- 01 Jan 1997 - 
TL;DR: An environment for comparative protein modeling is developed that consists of SWISS‐MODEL, a server for automated comparativeprotein modeling and of the SWiss‐PdbViewer, a sequence to structure workbench that provides a large selection of structure analysis and display tools.
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MOLMOL: a program for display and analysis of macromolecular structures.

TL;DR: Special efforts were made to allow for appropriate display and analysis of the sets of typically 20-40 conformers that are conventionally used to represent the result of an NMR structure determination, using functions for superimposing sets of conformers, calculation of root mean square distance (RMSD) values, identification of hydrogen bonds, and identification and listing of short distances between pairs of hydrogen atoms.
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AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR

TL;DR: The AQUA and PROCHECK-NMR programs provide a means of validating the geometry and restraint violations of an ensemble of protein structures solved by solution NMR, and their outputs include a detailed breakdown of the restraint violations.
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PRODRG: a tool for high-throughput crystallography of protein–ligand complexes

TL;DR: The small-molecule topology generator PRODRG is described, which takes input from existing coordinates or various two-dimensional formats and automatically generates coordinates and molecular topologies suitable for X-ray refinement of protein-ligand complexes.
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Protein backbone angle restraints from searching a database for chemical shift and sequence homology

TL;DR: TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence, and these averages can reliably be used as angular restraints for the protein whose structure is being studied.
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