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7OKT

X-ray structure of soluble EPCR in C2221 space group

Summary for 7OKT
Entry DOI10.2210/pdb7okt/pdb
DescriptorEndothelial protein C receptor, alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
Functional Keywordsmhc class i-like, phospholipid, anticoagulant, endothelial cell membrane receptor, lipid binding protein
Biological sourceHomo sapiens (human)
Total number of polymer chains2
Total formula weight47405.00
Authors
Erausquin, E.,Dichiara, M.G.,Lopez-Sagaseta, J. (deposition date: 2021-05-18, release date: 2022-04-27, Last modification date: 2024-10-09)
Primary citationErausquin, 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: 36068249
DOI: 10.1038/s41598-022-18844-y
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

227111

數據於2024-11-06公開中

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