A molecular dynamics study of the interaction between domain I-BAR of the IRSp53 protein and negatively charged membranes

The methods of computer simulation in all-atom and coarse-grained approximations have been used to study specific interactions of the isolated domain I-BAR of the actin-binding protein IRSp53 with model membranes containing neutral phospholipids and those including negatively charged PI(4,5)P 2 phos...

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Bibliographic Details
Published in:Biophysics (Oxford) 2011-04, Vol.56 (2), p.220-224
Main Authors: Levtsova, O. V., Davletov, I. D., Sokolova, O. S., Shaitan, K. V.
Format: Article
Language:English
Subjects:
Biological and Medical Physics
Biophysics
Membranes
Molecular biology
Molecular Biophysics
Physics
Physics and Astronomy
Proteins
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Summary:The methods of computer simulation in all-atom and coarse-grained approximations have been used to study specific interactions of the isolated domain I-BAR of the actin-binding protein IRSp53 with model membranes containing neutral phospholipids and those including negatively charged PI(4,5)P 2 phospholipids. It has been shown that the I-BAR domain does not interact with neutral lipids but induces bending of the synthetic membrane rich in negatively charged phospholipids. Clustering of charged lipids on the surface of the membrane at the sites of its interaction with the protein has been observed. This indicates that the interaction of I-BAR with negatively charged lipids is of electrostatic and hydrophobic nature.
ISSN:0006-3509
1555-6654
DOI:10.1134/S0006350911020199