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Structural Basis for Pattern Recognition by the Receptor for Advanced Glycation End Products (RAGE)
Open accessAbstract
The receptor for advanced glycated end products (RAGE) is a multiligand receptor that is implicated in the pathogenesis of various diseases, including diabetic complications, neurodegenerative disorders, and inflammatory responses. The ability of RAGE to recognize advanced glycated end products (AGEs) formed by nonenzymatic glycoxidation of cellular proteins places RAGE in the category of pattern recognition receptors. The structural mechanism of AGE recognition was an enigma due to the diversity of chemical structures found in AGE-modified proteins. Here, using NMR spectroscopy we showed that the immunoglobulin V-type domain of RAGE is responsible for recognizing various classes of AGEs. Three distinct surfaces of the V domain were identified to mediate AGE-V domain interactions. They are located in the positively charged areas of the V domain. The first interaction surface consists of strand C and loop CC ', the second interaction surface consists of strand C ', strand F, and loop FG, and the third interaction surface consists of strand A ' and loop EF. The secondary structure elements of the interaction surfaces exhibit significant flexibility on the ms-micros time scale. Despite highly specific AGE-V domain interactions, the binding affinity of AGEs for an isolated V domain is low, approximately 10 microm. Using in-cell fluorescence resonance energy transfer we show that RAGE is a constitutive oligomer on the plasma membrane. We propose that constitutive oligomerization of RAGE is responsible for recognizing patterns of AGE-modified proteins with affinities less than 100 nm.
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“In contrast to the aforementioned reports, circulating AGE levels could not be identified as an independent risk factor for cardiovascular or renal outcomes in diabetic subjects with diabetic nephropathy (524) , and circulating AGE levels were even inversely correlated with mortality in haemodialysis patients, the latter most probably due to a better nutritional status (525) .”
From Dietary factors and low-grade inflammation in relation to overweight and obesity (2011) · cites this paper as [524]
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Metadata
- Authors
- Xie, J., Reverdatto, S., Frolov, A., Hoffmann, R., Burz, D. S., & Shekhtman, A.
- Affiliations
- State University of New York (US)
- Leipzig University (DE)
- Corresponding author
- Shekhtman, Alexander
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2008-10
- Volume
- 283
- Issue
- 40
- Pages
- 27255-27269
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2038792388
- Cited by
- 252
- References
- 81
- Citations by year
- 2026: 6 · 2025: 12 · 2024: 11 · 2023: 15 · 2022: 16 · 2021: 13 · 2020: 14 · 2019: 15 · 2018: 10 · 2017: 8 · 2016: 15 · 2015: 13 · 2014: 13 · 2013: 22 · 2012: 17
- FWCI
- 11.52
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- American Diabetes Association
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- receptor for advanced glycation end products, RAGE, advanced glycation end products, pattern recognition receptors, protein-protein interaction surfaces, plasma membrane, binding affinity, diabetes complications, neurodegenerative diseases, inflammation
- MeSH terms
- Receptor for Advanced Glycation End Products, Cell Line, Humans, Inflammation, Magnetic Resonance Spectroscopy, Protein Binding, Structure-Activity Relationship, Glycation End Products, Advanced, Protein Structure, Secondary, Protein Structure, Tertiary, Neurodegenerative Diseases, Protein Structure, Quaternary, Diabetes Complications
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