Abstract:
:Molecular dynamics simulations may be used to probe the interactions of membrane proteins with lipids and with detergents at atomic resolution. Examples of such simulations for ion channels and for bacterial outer membrane proteins are described. Comparison of simulations of KcsA (an alpha-helical bundle) and OmpA (a beta-barrel) reveals the importance of two classes of side chains in stabilizing interactions with the head groups of lipid molecules: (i) tryptophan and tyrosine; and (ii) arginine and lysine. Arginine residues interacting with lipid phosphate groups play an important role in stabilizing the voltage-sensor domain of the KvAP channel within a bilayer. Simulations of the bacterial potassium channel KcsA reveal specific interactions of phosphatidylglycerol with an acidic lipid-binding site at the interface between adjacent protein monomers. A combination of molecular modelling and simulation reveals a potential phosphatidylinositol 4,5-bisphosphate-binding site on the surface of Kir6.2.
journal_name
Biochem Soc Transjournal_title
Biochemical Society transactionsauthors
Sansom MS,Bond PJ,Deol SS,Grottesi A,Haider S,Sands ZAdoi
10.1042/BST20050916keywords:
subject
Has Abstractpub_date
2005-11-01 00:00:00pages
916-20issue
Pt 5eissn
0300-5127issn
1470-8752pii
BST20050916journal_volume
33pub_type
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