title: Molecular Details of the PH Domain of ACAP1BAR-PHProtein Binding to PIP-Containing Membrane.
abstract: ACAP1 proteins were previously reported to specifically bind PIP2-containing cell membranes and form well-structured protein lattices in order to conduct membrane tubulation. We carried out molecular dynamics simulations to characterize orientation of the PH domains with respect to the BAR domains inside the protein dimer. Followed by molecular dynamics simulations, we present a comprehensive orientation analysis of PH domain under different states including unbound and bound with lipids. We have examined two binding pockets on the PH domain and present PMF profiles of the two pockets to account for their preference to PIP2lipids. Combining orientation analysis and studies of binding pockets, our simulations results reveal valuable molecular basis for protein-lipid interactions of ACAP1 proteins during membrane remodeling process.
authors.affiliation: Department of Physics and Materials Science, City University of Hong Kong , Hong Kong, China.
authors.forename: Kevin Chun
authors.initials: KC
authors.lastname: Chan
authors.affiliation: School of Biological Sciences, Nanyang Technological University , 639798, Singapore.
authors.forename: Lanyuan
authors.initials: L
authors.lastname: Lu
authors.affiliation: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences , Beijing 100101, China.|Center for Biological Imaging, Institute of Biophysics, Chinese Academy of Sciences , Beijing 100101, China.
authors.forename: Fei
authors.initials: F
authors.lastname: Sun
authors.affiliation: Department of Physics and Materials Science, City University of Hong Kong , Hong Kong, China.|City University of Hong Kong Shenzhen Research Institute , Shenzhen 518057, China.|Center for Advanced Nuclear Safety and Sustainable Development, City University of Hong Kong , Hong Kong, China.
authors.forename: Jun
authors.identifier: 0000-0001-8227-9671
authors.initials: J
authors.lastname: Fan
mesh_terms: D020690:GTPase-Activating Proteins / Q000737:chemistry*; D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry*; D008055:Lipids / Q000737:chemistry; D056004:Molecular Dynamics Simulation; D000070539:Pleckstrin Homology Domains
chemical_list: C507017:ACAP1 protein, human; D020690:GTPase-Activating Proteins; D008051:Lipid Bilayers; D008055:Lipids