title: The potassium channel KcsA: a model protein in studying membrane protein oligomerization and stability of oligomeric assembly?
abstract: Many membrane proteins are functional as stable oligomers. An understanding of the conditions that elicit and enhance oligomerization is important in many therapeutics. In this regard, protein-protein and protein-lipid interactions play crucial roles in the assembly and stability of oligomeric complexes. Recent years have seen a rapid increase in the mechanistic information on the importance of cytoplasmic termini in determining subunit assembly and stability of oligomeric complexes. In addition, the role of specific protein-lipid interaction between anionic phospholipids and "hot spots" on the protein surface has also become evident in stabilizing oligomeric assemblies. This review focuses on several contemporary developments of membrane proteins that stabilize oligomers by taking the potassium channel KcsA as an exemplary ion channel.
authors: School of Molecular and Systems Medicine, Alberta Diabetes Institute, University of Alberta, Edmonton, Canada. mraja@pmcol.ualberta.ca
authors: Mobeen
authors: M
authors: Raja
mesh_terms: D000818:Animals; D001419:Bacteria / Q000737:chemistry / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008563:Membrane Lipids / Q000378:metabolism*; D008958:Models, Molecular; D015221:Potassium Channels / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D055503:Protein Multimerization; D055550:Protein Stability
chemical_list: D001426:Bacterial Proteins; D008563:Membrane Lipids; D015221:Potassium Channels; C107790:prokaryotic potassium channel