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
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