Linked Life Data

19917228

Source:http://linkedlifedata.com/resource/pubmed/id/19917228

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2009-11-17
pubmed:abstractText
The structure of the endophilin N-terminal amphipathic helix Bin/Amphiphysin/Rvs-homology (N-BAR) domain is unique because of an additional insert helix under the arch of the N-BAR dimer. The structure of this additional helix has not been fully resolved in crystallographic studies, and thus presents a challenge to molecular-level analysis. Large-scale molecular-dynamics simulations were therefore employed to investigate the interaction of a single endophilin N-BAR with a lipid bilayer. Various possible configurations of the additional insert helix under the top of the arch of the endophilin N-BAR were modeled to examine their effect on membrane bending. A residue-residue and residue-lipid headgroup distance analysis, similar to that performed with electron paramagnetic resonance spectroscopy, revealed that the insert helix remains perpendicular to the long axis of the N-BAR over the duration of the simulations. It was also found that the degree of membrane bending is directly related to the orientation of the additional insert helix, and that the perpendicular configuration generates the largest curvature consistent with mutation experiments. In addition, the angle formed between the two N-BAR monomers at the top of the arch is sensitive to the orientation of the insert helices. A membrane sensing-binding-bending mechanism is proposed to describe the process of an endophilin N-BAR interaction with a membrane.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1542-0086
pubmed:author
pubmed:issnType
Electronic
pubmed:day
18
pubmed:volume
97
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2746-53
pubmed:dateRevised
2010-11-22
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Membrane binding by the endophilin N-BAR domain.
pubmed:affiliation
Center of Biophysical Modeling and Simulation, University of Utah, Salt Lake City, Utah, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural