title: [A molecular dynamics study of the interaction between domain I-BAR of the IRSp53 protein and negatively charged membranes].
abstract: The methods of computer simulation in full-atomic and large-grain approximations have been used to study specific interactions of the isolated domain I-BAR of the actin-binding protein IRSp53 and model membranes containing neutral phospholipids, as well as membranes containing high amounts of negatively charged PI(4,5)P2 phospholipids. It has been shown that the I-BAR domain does not interact with neutral lipids but induces the bending of the synthetic membrane rich in negatively charged phospholipids. A clusterization 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 the I-BAR protein with negatively charged lipids is of electrostatic and hydrophobic nature.
authors.forename: O V
authors.initials: OV
authors.lastname: Levtsova
authors.forename: I D
authors.initials: ID
authors.lastname: Davletov
authors.forename: O S
authors.initials: OS
authors.lastname: Sokolova
authors.forename: K V
authors.initials: KV
authors.lastname: Shaĭtan
mesh_terms: D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008567:Membranes, Artificial; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000378:metabolism; D010743:Phospholipids / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D055672:Static Electricity
chemical_list: C119539:BAIAP2 protein, human; D008567:Membranes, Artificial; D009419:Nerve Tissue Proteins; D010743:Phospholipids