Cargando…
Insertion of the Ca(2+)-Independent Phospholipase A(2) into a Phospholipid Bilayer via Coarse-Grained and Atomistic Molecular Dynamics Simulations
Group VI Ca(2+)-independent phospholipase A(2) (iPLA(2)) is a water-soluble enzyme that is active when associated with phospholipid membranes. Despite its clear pharmaceutical relevance, no X-ray or NMR structural information is currently available for the iPLA(2) or its membrane complex. In this pa...
Autores principales: | Bucher, Denis, Hsu, Yuan-Hao, Mouchlis, Varnavas D., Dennis, Edward A., McCammon, J. Andrew |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3723492/ https://www.ncbi.nlm.nih.gov/pubmed/23935474 http://dx.doi.org/10.1371/journal.pcbi.1003156 |
Ejemplares similares
-
Lipoprotein-associated phospholipase A(2): A paradigm for allosteric regulation by membranes
por: Mouchlis, Varnavas D., et al.
Publicado: (2022) -
Substrate-Specific
Inhibition Constants for Phospholipase
A(2) Acting on Unique Phospholipid Substrates in Mixed Micelles
and Membranes Using Lipidomics
por: Mouchlis, Varnavas D., et al.
Publicado: (2019) -
Membrane Association
Allosterically Regulates Phospholipase
A(2) Enzymes and Their Specificity
por: Mouchlis, Varnavas D., et al.
Publicado: (2022) -
Membrane
Allostery and Unique Hydrophobic Sites Promote
Enzyme Substrate Specificity
por: Mouchlis, Varnavas D., et al.
Publicado: (2018) -
Omega-3 versus Omega-6 fatty acid availability is controlled by hydrophobic site geometries of phospholipase A(2)s
por: Hayashi, Daiki, et al.
Publicado: (2021)