Journal of Molecular Biology
Volume 423, Issue 5, 9 November 2012, Pages 800-817
Membrane Binding and Self-Association of the Epsin N-Terminal Homology Domain
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open access
Graphical Abstract
Highlights
► ENTH domain plays an essential role in clathrin-mediated endocytosis. ► Membrane binding of ENTH domain is studied by a combined MD and EPR approach. ► A CG ENTH model for CG MD simulations is developed. ► ENTH-bound membrane tubules and vesicles are studied via CG MD simulations. ► The arrangement of ENTH domains highly correlates with local membrane curvature.
Abbreviations
ENTH
epsin N-terminal homology
PIP2
phosphatidylinositol 4,5-bisphosphate
CG
coarse-grained
MD
molecular dynamics
CME
clathrin-mediated endocytosis
N-BAR
N-terminal Bin/Amphiphysin/Rvs-homology
EM
electron microscopy
HAS
hybrid analytical systematic
PMF
potential of mean force
RT
room temperature
Keywords
epsin
ENTH domain
molecular dynamics
membrane remodeling
amphipathic helix binding
Cited by (0)
- †
C.-L.L. and C.C.J. contributed equally to this work.
Copyright © 2012 Elsevier Ltd.