Molecular Details of the PH Domain of ACAP1BAR-PH Protein Binding to PIP-Containing Membrane

Research output: Journal Publications and Reviews (RGC: 21, 22, 62)21_Publication in refereed journalpeer-review

11 Scopus Citations
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Detail(s)

Original languageEnglish
Pages (from-to)3586-3596
Journal / PublicationJournal of Physical Chemistry B
Volume121
Issue number15
Online published16 Jan 2017
Publication statusPublished - 20 Apr 2017

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 PIP2 lipids. 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.

Research Area(s)

  • PLECKSTRIN HOMOLOGY DOMAINS, DYNAMICS SIMULATIONS, SIGNALING PROTEINS, FORCE-FIELD, CURVATURE, MECHANISM, CHARMM, RECOGNITION, TUBULATION, COMPLEXES