Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 510, Issue 1, Pages 1-10Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2011.03.010
Keywords
Membrane proteins; Oligomerization; Potassium channel KcsA; Electrostatic interaction; Anionic phospholipids; Hot spots; Cytoplasmic termini; Tryptophan residues; Protein-lipid interaction; Supramolecular complexes
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Funding
- Chemical Sciences Division (CW) of the Netherlands Organization for Scientific Research (NWO)
- Sigrid Juselius Foundation
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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. (C) 2011 Elsevier Inc. All rights reserved.
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