Structure and Workings of Receptor Tied to Inflammation and Cell Death Seen for First Time

Structure and Workings of Receptor Tied to Inflammation and Cell Death Seen for First Time

Publication date: Oct 08, 2019

Scientists observed for the first time the molecular structure of the P2X receptor, a protein that plays a key role in cell death, inflammation, and cancer progression. Investigators at Oregon Health & Science University (OSHU) used a technique called cryogenic electron microscopy (cryo-EM) to see for the first time the 3D molecular structure of the cytoplasmic domain of the P2X receptor in action. In this way, they found the cytoplasmic domain of P2X was bound to several groups of fatty acid molecules, a chemical modification known as palmitoylation (the addition of palmitoyl groups). -Our structures provide first insights into the architecture and function of a P2X receptor cytoplasmic domain,” the team wrote.

Concepts Keywords
Calcium Key death inflammation
Cancer Disorders P2X
Cardiovascular Branches of biology
Cations Proteins
Coronary Artery Disease Ion channels
Cryogenic Electron Microscopy Integral membrane proteins
Electrical Charge Protein families
Extracellular Transport proteins
Fatty Acid P2X purinoreceptor
Guanosine Palmitoylation
Inflammation Ligand-gated ion channel
Ion Channels P2RX7
Molecular Receptors P2RX4
Neurodegeneration
Neuroprotective
Nucleoside
Palmitoyl
Palmitoylation
PhD
Receptors
Sodium
White

Semantics

Type Source Name
gene UNIPROT ITGBL1
disease MESH Inflammation
disease MESH cancer
disease DOID cancer
disease MESH sclerosis
disease MESH coronary artery disease
disease DOID coronary artery disease
drug DRUGBANK Calcium
gene UNIPROT REST
drug DRUGBANK Hexadecanal
gene UNIPROT PDC
pathway BSID Release
drug DRUGBANK Guanosine

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