2M1K
Interaction of Human S100A6 (C3S) with V domain of Receptor for Advanced Glycation End products (RAGE)
Summary for 2M1K
| Entry DOI | 10.2210/pdb2m1k/pdb |
| Related | 1K9K 2E5E |
| NMR Information | BMRB: 18868 |
| Descriptor | Protein S100-A6, Advanced glycosylation end product-specific receptor (2 entities in total) |
| Functional Keywords | s100a6 c3s, rage v, heterotetrameric, haddock model, protein binding |
| Biological source | Homo sapiens (human) More |
| Cellular location | Nucleus envelope: P06703 Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted. Isoform 10: Cell membrane ; Single-pass type I membrane protein : Q15109 |
| Total number of polymer chains | 4 |
| Total formula weight | 42789.34 |
| Authors | Gupta, A.A.,Yu, C. (deposition date: 2012-11-29, release date: 2015-03-25, Last modification date: 2024-11-06) |
| Primary citation | Mohan, S.K.,Gupta, A.A.,Yu, C. Interaction of the S100A6 mutant (C3S) with the V domain of the receptor for advanced glycation end products (RAGE). Biochem.Biophys.Res.Commun., 434:328-333, 2013 Cited by PubMed Abstract: S100A6 is involved in several vital biological functions, such as calcium sensing and cell proliferation. It is a homodimeric protein that belongs to the S100 protein family. The receptor for advanced glycation end products (RAGE) has been shown to play a role in the progression of various disease conditions, such as diabetes and immune/inflammatory disorders. Information regarding the association of RAGE with S100 proteins at a molecular level is useful to understand the diversity of the RAGE signaling pathways. In this report, biomolecular NMR techniques were utilized for the resonance assignment of the C3S mutation in human S100A6 and characterizing its interaction with the RAGE V domain. Further binding affinity between S100A6m and the RAGE V domain was determined by isothermal titration calorimetric studies. HADDOCK was used to generate a heterotetramer model of the S100A6m-RAGE V domain complex. This model provides an important insights into the S100-RAGE cellular signaling pathway. PubMed: 23537648DOI: 10.1016/j.bbrc.2013.03.049 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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