The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding

Lipoprotein lipase (LPL) undergoes spontaneous inactivation via global unfolding and this unfolding is prevented by GPIHBP1 (Mysling et al., 2016). We now show: (1) that ANGPTL4 inactivates LPL by catalyzing the unfolding of its hydrolase domain; (2) that binding to GPIHBP1 renders LPL largely refra...

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Bibliografische gegevens
Gepubliceerd in:eLife
Hoofdauteurs: Mysling, Simon, Kristensen, Kristian Kølby, Larsson, Mikael, Kovrov, Oleg, Bensadouen, André, Jørgensen, Thomas JD, Olivecrona, Gunilla, Young, Stephen G, Ploug, Michael
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: eLife Sciences Publications, Ltd 2016
Onderwerpen:
Biophysics and Structural Biology
Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC5148603/
https://ncbi.nlm.nih.gov/pubmed/27929370
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.7554/eLife.20958
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