scholarly journals The Interfacial Lipid Binding Site on the Potassium Channel KcsA Is Specific for Anionic Phospholipids

2005 ◽  
Vol 89 (6) ◽  
pp. 4081-4089 ◽  
Author(s):  
Phedra Marius ◽  
Simon J. Alvis ◽  
J. Malcolm East ◽  
Anthony G. Lee
Keyword(s):  
Potassium Channel ◽  
Binding Site ◽  
Lipid Binding ◽  
Anionic Phospholipids ◽  
Potassium Channel Kcsa ◽  
Lipid Binding Site

scholarly journals Modulation of the potassium channel KcsA by anionic phospholipids: Role of arginines at the non-annular lipid binding sites

2019 ◽  
Vol 1861 (10) ◽  
pp. 183029 ◽  
Author(s):  
José A. Poveda ◽  
A. Marcela Giudici ◽  
M. Lourdes Renart ◽  
Oscar Millet ◽  
Andrés Morales ◽  
...  
Keyword(s):  
Potassium Channel ◽  
Binding Sites ◽  
Lipid Binding ◽  
Anionic Phospholipids ◽  
Potassium Channel Kcsa

scholarly journals Characterizing the Fatty Acid Binding Site in the Cavity of Potassium Channel KcsA

Biochemistry ◽  
2012 ◽  
Vol 51 (40) ◽  
pp. 7996-8002 ◽  
Author(s):  
Natalie Smithers ◽  
Juan H. Bolivar ◽  
Anthony G. Lee ◽  
J. Malcolm East
Keyword(s):  
Fatty Acid ◽  
Potassium Channel ◽  
Binding Site ◽  
Fatty Acid Binding ◽  
Potassium Channel Kcsa ◽  
Fatty Acid Binding Site

The N-Terminus is the Lipid-Binding Site of SAA: Supporting Evidence by MoAbs

1991 ◽  
pp. 83-86
Author(s):  
Yifat Ziq-Bachar ◽  
David Levartowsky ◽  
Mordechaipras ◽  
Alistair F. Strachan ◽  
Mati Fridkin ◽  
...  
Keyword(s):  
Binding Site ◽  
Lipid Binding ◽  
Supporting Evidence ◽  
N Terminus ◽  
Lipid Binding Site

Molecular simulations and lipid–protein interactions: potassium channels and other membrane proteins

2005 ◽  
Vol 33 (5) ◽  
pp. 916-920 ◽  
Author(s):  
M.S.P. Sansom ◽  
P.J. Bond ◽  
S.S. Deol ◽  
A. Grottesi ◽  
S. Haider ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Binding Site ◽  
Protein Interactions ◽  
Outer Membrane Proteins ◽  
Lipid Binding ◽  
Potassium Channel Kcsa ◽  
Head Groups ◽  
Arginine Residues ◽  
Lipid Protein Interactions ◽  
Dynamics Simulations

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 α-helical bundle) and OmpA (a β-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.

Identification of the Lipid-Binding Site of Phosphatidylcholine-Transfer Protein with Phosphatidylcholine Analogs Containing Photactivable Carbene Precursors

1983 ◽  
Vol 132 (2) ◽  
pp. 441-449 ◽  
Author(s):  
Jan WESTERMAN ◽  
Karel W. A. WIRTZ ◽  
Theo BERKHOUT ◽  
Laurens L. M. DEENEN ◽  
Ramachandran RADHAKRISHNAN ◽  
...  
Keyword(s):  
Binding Site ◽  
Lipid Binding ◽  
Transfer Protein ◽  
Phosphatidylcholine Transfer Protein ◽  
Lipid Binding Site

scholarly journals Phospholipid-induced structural changes to an erythroid β spectrin ankyrin-dependent lipid-binding site

2008 ◽  
Vol 1778 (11) ◽  
pp. 2612-2620 ◽  
Author(s):  
Aleksander Czogalla ◽  
Krzysztof Grzymajło ◽  
Adam Jezierski ◽  
Aleksander F. Sikorski
Keyword(s):  
Binding Site ◽  
Structural Changes ◽  
Lipid Binding ◽  
Lipid Binding Site

scholarly journals Human TRPC5 structures reveal interaction of a xanthine-based TRPC1/4/5 inhibitor with a conserved lipid binding site

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
David J. Wright ◽  
Katie J. Simmons ◽  
Rachel M. Johnson ◽  
David J. Beech ◽  
Stephen P. Muench ◽  
...  
Keyword(s):  
Binding Site ◽  
Lipid Binding ◽  
Structural Basis ◽  
Chemical Probes ◽  
Endogenous Factors ◽  
Drug Candidates ◽  
Channel Regulation ◽  
Exogenous Factors ◽  
Translational Studies ◽  
Lipid Binding Site

AbstractTRPC1/4/5 channels are non-specific cation channels implicated in a wide variety of diseases, and TRPC1/4/5 inhibitors have recently entered clinical trials. However, fundamental and translational studies require a better understanding of TRPC1/4/5 channel regulation by endogenous and exogenous factors. Although several potent and selective TRPC1/4/5 modulators have been reported, the paucity of mechanistic insights into their modes-of-action remains a barrier to the development of new chemical probes and drug candidates. Xanthine-based modulators include the most potent and selective TRPC1/4/5 inhibitors described to date, as well as TRPC5 activators. Our previous studies suggest that xanthines interact with a, so far, elusive pocket of TRPC1/4/5 channels that is essential to channel gating. Here we report the structure of a small-molecule-bound TRPC1/4/5 channel—human TRPC5 in complex with the xanthine Pico145—to 3.0 Å. We found that Pico145 binds to a conserved lipid binding site of TRPC5, where it displaces a bound phospholipid. Our findings explain the mode-of-action of xanthine-based TRPC1/4/5 modulators, and suggest a structural basis for TRPC1/4/5 modulation by endogenous factors such as (phospho)lipids and Zn2+ ions. These studies lay the foundations for the structure-based design of new generations of TRPC1/4/5 modulators.

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