The Extracellular Region of the Receptor for Advanced Glycation End Products Is Composed of Two Independent Structural Units
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...
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Published in | Biochemistry (Easton) Vol. 46; no. 23; pp. 6957 - 6970 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
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United States
American Chemical Society
12.06.2007
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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 ∼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 biochemical methods including limited proteolysis, dynamic light scattering, CD, and NMR. A homology model of sRAGE was constructed to aid in the interpretation of the experimental data. Our results show that the V and C1 domains are not independent domains, but rather form an integrated structural unit. In contrast, C2 is attached to VC1 by a flexible linker and is fully independent. The interaction with a known RAGE ligand, Ca2+-S100B, was mapped to VC1, with the major contribution from the V domain but clearly defined secondary effects from the C1 domain. The implications of these results are discussed with respect to models for RAGE signaling. |
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AbstractList | 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 ∼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 biochemical methods including limited proteolysis, dynamic light scattering, CD, and NMR. A homology model of sRAGE was constructed to aid in the interpretation of the experimental data. Our results show that the V and C1 domains are not independent domains, but rather form an integrated structural unit. In contrast, C2 is attached to VC1 by a flexible linker and is fully independent. The interaction with a known RAGE ligand, Ca2+-S100B, was mapped to VC1, with the major contribution from the V domain but clearly defined secondary effects from the C1 domain. The implications of these results are discussed with respect to models for RAGE signaling. 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 biochemical methods including limited proteolysis, dynamic light scattering, CD, and NMR. A homology model of sRAGE was constructed to aid in the interpretation of the experimental data. Our results show that the V and C1 domains are not independent domains, but rather form an integrated structural unit. In contrast, C2 is attached to VC1 by a flexible linker and is fully independent. The interaction with a known RAGE ligand, Ca2+-S100B, was mapped to VC1, with the major contribution from the V domain but clearly defined secondary effects from the C1 domain. The implications of these results are discussed with respect to models for RAGE signaling. |
Author | Fritz, Günter Dattilo, Brian M Chazin, Walter J Leclerc, Estelle Heizmann, Claus W Vander Kooi, Craig W |
Author_xml | – sequence: 1 givenname: Brian M surname: Dattilo fullname: Dattilo, Brian M – sequence: 2 givenname: Günter surname: Fritz fullname: Fritz, Günter – sequence: 3 givenname: Estelle surname: Leclerc fullname: Leclerc, Estelle – sequence: 4 givenname: Craig W surname: Vander Kooi fullname: Vander Kooi, Craig W – sequence: 5 givenname: Claus W surname: Heizmann fullname: Heizmann, Claus W – sequence: 6 givenname: Walter J surname: Chazin fullname: Chazin, Walter J |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/17508727$$D View this record in MEDLINE/PubMed |
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Notes | istex:25F7176EC781D38812443439B6BAEA44B281C7C6 ark:/67375/TPS-FX2PG13X-C This work was supported by grants from the U.S. National Institutes of Health (RO1 GM62112 to W.J.C.; T32 GM08320 to the Vanderbilt Molecular Biophysics Training Program for support of B.M.D.; P30 ES000267 to the Vanderbilt Center in Molecular Toxicology and P50 CA068485 to the Vanderbilt-Ingram Cancer Center for support of facilities; 5P60 DK20593 to the Vanderbilt Diabetes Research and Training Center for funding a pilot project). G.F., E.L., and C.W.H. were supported by the Deutsche Forschungsgemeinschaft (Transregio-SFB 11). C.W.V.K. is a Leukemia and Lymphoma Society Fellow. ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
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(bi7003735b00053/bi7003735b00053_1) 2005; 88 Srikrishna G. (bi7003735b00060/bi7003735b00060_1) 2002; 80 Miyata T. (bi7003735b00010/bi7003735b00010_1) 1996; 98 Ikeda K. (bi7003735b00007/bi7003735b00007_1) 1996 Hanford L. E. (bi7003735b00038/bi7003735b00038_1) 2004; 279 Yamagishi S. (bi7003735b00019/bi7003735b00019_1) 2003; 23 Yan S. D. (bi7003735b00003/bi7003735b00003_1) 1994; 269 Bork P. (bi7003735b00041/bi7003735b00041_1) 1994; 242 Abbreviations RAGE (bi7003735n00001/bi7003735n00001_1) Sorci G. (bi7003735b00014/bi7003735b00014_1) 2003 Ishihara K. (bi7003735b00064/bi7003735b00064_1) 2003; 550 Stern D. (bi7003735b00018/bi7003735b00018_1) 2002; 54 Livnah O. (bi7003735b00061/bi7003735b00061_1) 1999 Pervushin K. (bi7003735b00047/bi7003735b00047_1) 1997 |
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Snippet | The receptor for advanced glycation end products (RAGE) is an important cell surface receptor being pursued as a therapeutic target because it has been... |
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SubjectTerms | Amino Acid Sequence Base Sequence Cloning, Molecular DNA - chemistry DNA - genetics Escherichia coli - genetics Glycation End Products, Advanced - chemistry Glycation End Products, Advanced - metabolism Humans Models, Molecular Molecular Sequence Data Peptide Fragments - chemistry Protein Conformation Receptor for Advanced Glycation End Products Receptors, Immunologic - chemistry Receptors, Immunologic - genetics Receptors, Immunologic - metabolism Recombinant Proteins - chemistry Recombinant Proteins - metabolism |
Title | The Extracellular Region of the Receptor for Advanced Glycation End Products Is Composed of Two Independent Structural Units |
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