Cargando…
Structure of the lipoprotein lipase–GPIHBP1 complex that mediates plasma triglyceride hydrolysis
Lipoprotein lipase (LPL) is responsible for the intravascular processing of triglyceride-rich lipoproteins. The LPL within capillaries is bound to GPIHBP1, an endothelial cell protein with a three-fingered LU domain and an N-terminal intrinsically disordered acidic domain. Loss-of-function mutations...
Autores principales: | Birrane, Gabriel, Beigneux, Anne P., Dwyer, Brian, Strack-Logue, Bettina, Kristensen, Kristian Kølby, Francone, Omar L., Fong, Loren G., Mertens, Haydyn D. T., Pan, Clark Q., Ploug, Michael, Young, Stephen G., Meiyappan, Muthuraman |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
National Academy of Sciences
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6358717/ https://www.ncbi.nlm.nih.gov/pubmed/30559189 http://dx.doi.org/10.1073/pnas.1817984116 |
Ejemplares similares
-
Lipoprotein lipase is active as a monomer
por: Beigneux, Anne P., et al.
Publicado: (2019) -
A protein of capillary endothelial cells, GPIHBP1, is crucial for plasma triglyceride metabolism
por: Young, Stephen G., et al.
Publicado: (2022) -
The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain
por: Mysling, Simon, et al.
Publicado: (2016) -
The crystal structure of human microsomal triglyceride transfer protein
por: Biterova, Ekaterina I., et al.
Publicado: (2019) -
The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding
por: Mysling, Simon, et al.
Publicado: (2016)