4E99
Human Serum Albumin Complex with Perfluorooctane Sulfonate Potassium
Summary for 4E99
| Entry DOI | 10.2210/pdb4e99/pdb |
| Descriptor | Serum albumin, heptadecafluoro-1-octanesulfonic acid (3 entities in total) |
| Functional Keywords | plasma protein, transporter, drug binding, extracellular, transport protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted: P02768 |
| Total number of polymer chains | 1 |
| Total formula weight | 67571.48 |
| Authors | Luo, Z.P.,Shi, X.L.,Huang, M.D. (deposition date: 2012-03-20, release date: 2012-06-06, Last modification date: 2023-11-08) |
| Primary citation | Luo, Z.P.,Shi, X.L.,Hu, Q.,Zhao, B.,Huang, M.D. Structural evidence of perfluorooctane sulfonate transport by human serum albumin Chem.Res.Toxicol., 25:990-992, 2012 Cited by PubMed Abstract: Perfluorooctane sulfonate (PFOS) is a man-made fluorosurfactant and globally persistent organic pollutant. PFOS is mainly distributed in blood with a long half-life for elimination. PFOS was found mainly bound to human serum albumin (HSA) in plasma, the most abundant protein in human blood plasma, which transports a variety of endogenous and exogenous ligands. However, the structural basis of such binding remains unclear. Here, we report the crystal structure of the HSA-PFOS complex and show that PFOS binds to HSA at a molar ratio of 2:1. In addition, PFOS binding renders the HSA structure more compact. Our results provide a structural mechanism to understand the retention of surfactants in human serum. PubMed: 22482699DOI: 10.1021/tx300112p PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
Download full validation report
