• Title of article

    The potassium channel KcsA: A model protein in studying membrane protein oligomerization and stability of oligomeric assembly?

  • Author/Authors

    Raja، نويسنده , , Mobeen، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2011
  • Pages
    10
  • From page
    1
  • To page
    10
  • 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.
  • Keywords
    membrane proteins , Electrostatic Interaction , Potassium channel KcsA , anionic phospholipids , hot spots , Tryptophan residues , Cytoplasmic termini , protein–lipid interaction , supramolecular complexes , oligomerization
  • Journal title
    Archives of Biochemistry and Biophysics
  • Serial Year
    2011
  • Journal title
    Archives of Biochemistry and Biophysics
  • Record number

    1632224