Modeling of an ion channel in its open conformation.
|Abstract||We have modeled the structure of KirBac1.1 in an open state using as a starting point the structure of KirBac1.1 in its closed conformation (Protein Data Bank 1P7B). To test the validity of the open-state model, molecular dynamics simulations in octane, a lipid bilayer mimetic, were carried out. Simulations of the closed conformer were used for comparison purposes. The total simulation time was approximately 138 ns. The initial open model was ref ... [truncated at 450 characters in length]|
|Author||Domene, Carmen; Doyle, Declan A; Vénien-Bryan, Catherine;|
|Subject||Biophysics Burkholderia pseudomallei Crystallography, X-Ray Databases, Protein Glycine Models, Molecular Phenylalanine Potassium Potassium Channels, Inwardly Rectifying Protein Conformation Protein Structure, Secondary methods metabolism chemistry chemistry chemistry chemistry|
Role of aromatic localization in the gating process of a potassium channel.
|Abstract||Position of the transmembrane aromatic residues of the KirBac1.1 potassium channel shifts from an even distribution in the closed state toward the membrane/solute interface in the open state model. This is the first example of an integral membrane protein making use of the observed preference for transmembrane aromatic residues to reside at the interfaces. The process of aromatic localization is proposed as a means of directing and stabilizing st ... [truncated at 450 characters in length]|
|Author||Domene, Carmen; Vemparala, Satyavani; Klein, Michael L; et al|
|Subject||Biophysics Cell Membrane Computer Simulation G Protein-Coupled Inwardly-Rectifying Potassium Channels Ion Channel Gating Lipid Bilayers Lipids Models, Molecular Molecular Conformation Phenylalanine Potassium Channels Time Factors Tyrosine methods metabolism chemistry chemistry chemistry chemistry chemistry chemistry|