Back to search

Article

Structure of Dimeric Lipoprotein Lipase Reveals a Pore for Hydrolysis of Acyl Chains

2023-03-22

Abstract excerpt

Lipoprotein lipase (LPL) hydrolyzes triglycerides from circulating lipoproteins, releasing free fatty acids. Active LPL is needed to prevent hypertriglyceridemia, which is a risk factor for cardiovascular disease (CVD). Using cryogenic electron microscopy (cryoEM), we determined the structure of an active LPL dimer at 3.9 Å resolution. This is the first structure of a mammalian lipase with an open, hydrophobic por...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work
a20a9525-a914-5edd-baf9-448af65a13c0
DOI
10.1101/2023.03.21.533650
Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest
Interactive article relationship graphSelect a related publication card to move it into the centre and load its closest explainable connections. Solid lines are source-backed structured connections. Dashed lines are semantic discovery signals and are not scientific evidence.
Structure of Dimeric Lipoprotein Lipase Reveals a Pore for Hydrolysis of Acyl ChainsDOI 10.1101/2023.03.21.533650
Select a neighboring publication to make it the new centre.