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Advanced glycation end product recognition by the receptor for AGEs.
- Source :
-
Structure (London, England : 1993) [Structure] 2011 May 11; Vol. 19 (5), pp. 722-32. - Publication Year :
- 2011
-
Abstract
- Nonenzymatic protein glycation results in the formation of advanced glycation end products (AGEs) that are implicated in the pathology of diabetes, chronic inflammation, Alzheimer's disease, and cancer. AGEs mediate their effects primarily through a receptor-dependent pathway in which AGEs bind to a specific cell surface associated receptor, the Receptor for AGEs (RAGE). N(ɛ)-carboxy-methyl-lysine (CML) and N(ɛ)-carboxy-ethyl-lysine (CEL), constitute two of the major AGE structures found in tissue and blood plasma, and are physiological ligands of RAGE. 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. Peptide backbone atoms make specific contacts with the V domain. The geometry of the bound CEL peptide is compatible with many CML (CEL)-modified sites found in plasma proteins. The structure explains how such patterned ligands as CML (CEL)-proteins bind to RAGE and contribute to RAGE signaling.<br /> (Copyright © 2011 Elsevier Ltd. All rights reserved.)
- Subjects :
- Alzheimer Disease metabolism
Alzheimer Disease pathology
Amino Acid Sequence
Binding Sites
Blood Proteins metabolism
Cloning, Molecular
Diabetes Mellitus metabolism
Diabetes Mellitus pathology
Dipeptides chemical synthesis
Escherichia coli
Glycation End Products, Advanced
Glycosylation
Inflammation metabolism
Inflammation pathology
Models, Molecular
Molecular Sequence Data
Neoplasms metabolism
Neoplasms pathology
Protein Conformation
Protein Structure, Tertiary
Receptor for Advanced Glycation End Products
Receptors, Immunologic genetics
Receptors, Immunologic metabolism
Recombinant Proteins genetics
Recombinant Proteins metabolism
Blood Proteins chemistry
Dipeptides metabolism
Receptors, Immunologic chemistry
Recombinant Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1878-4186
- Volume :
- 19
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Structure (London, England : 1993)
- Publication Type :
- Academic Journal
- Accession number :
- 21565706
- Full Text :
- https://doi.org/10.1016/j.str.2011.02.013