7OKV
Crystal structure of soluble EPCR after exposure to the nonionic surfactant Polysorbate 20
Summary for 7OKV
Entry DOI | 10.2210/pdb7okv/pdb |
Descriptor | Endothelial protein C receptor, 2-acetamido-2-deoxy-beta-D-glucopyranose, HEXADECANE, ... (7 entities in total) |
Functional Keywords | mhc class-i like, phospholipid, anticoagulant, endothelial cell membrane receptor, lipid binding protein |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 1 |
Total formula weight | 23381.32 |
Authors | Erausquin, E.,Dichiara, M.G.,Lopez-Sagaseta, J. (deposition date: 2021-05-18, release date: 2022-07-06, Last modification date: 2024-01-31) |
Primary citation | Erausquin, E.,Moran-Garrido, M.,Saiz, J.,Barbas, C.,Dichiara-Rodriguez, G.,Urdiciain, A.,Lopez-Sagaseta, J. Identification of a broad lipid repertoire associated to the endothelial cell protein C receptor (EPCR). Sci Rep, 12:15127-15127, 2022 Cited by PubMed Abstract: Evidence is mounting that the nature of the lipid bound to the endothelial cell protein C receptor (EPCR) has an impact on its biological roles, as observed in anticoagulation and more recently, in autoimmune disease. Phosphatidylethanolamine and phosphatidylcholine species dominate the EPCR lipid cargo, yet, the extent of diversity in the EPCR-associated lipid repertoire is still unknown and remains to be uncovered. We undertook mass spectrometry analyses to decipher the EPCR lipidome, and identified species not yet described as EPCR ligands, such as phosphatidylinositols and phosphatidylserines. Remarkably, we found further, more structurally divergent lipids classes, represented by ceramides and sphingomyelins, both in less abundant quantities. In support of our mass spectrometry results and previous studies, high-resolution crystal structures of EPCR in three different space groups point to a prevalent diacyl phospholipid moiety in EPCR's pocket but a mobile and ambiguous lipid polar head group. In sum, these studies indicate that EPCR can associate with varied lipid classes, which might impact its properties in anticoagulation and the onset of autoimmune disease. PubMed: 36068249DOI: 10.1038/s41598-022-18844-y PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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