scholarly journals 1-Oleoyl-2-acetylglycerol Stimulates 5-Lipoxygenase Activity via a Putative (Phospho)lipid Binding Site within the N-terminal C2-like Domain

2005 ◽  
Vol 280 (29) ◽  
pp. 26913-26921 ◽  
Author(s):  
Christina Hörnig ◽  
Dana Albert ◽  
Lutz Fischer ◽  
Michael Hörnig ◽  
Olof Rådmark ◽  
...  
Keyword(s):  
Binding Site ◽  
Lipid Binding ◽  
Lipoxygenase Activity ◽  
Phospho Lipid ◽  
Lipid 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

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.

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 Lipid Interactions of a Ciliary Membrane TRP Channel: Simulation and Structural Studies of Polycystin-2 (PC2)

2019 ◽  
Author(s):  
Qinrui Wang ◽  
George Hedger ◽  
Prafulla Aryal ◽  
Mariana Grieben ◽  
Chady Nasrallah ◽  
...  
Keyword(s):  
Binding Site ◽  
Trp Channels ◽  
Md Simulations ◽  
Lipid Binding ◽  
Cryoelectron Microscopy ◽  
Trpv1 Channel ◽  
Lipid Interactions ◽  
Dynamics Simulations ◽  
Phosphatidylinositol Phosphates ◽  
Lipid Binding Site

AbstractPolycystin-2 (PC2) is a member of the TRPP subfamily of TRP channels and is present in ciliary membranes of the kidney. PC2 can be either homo-tetrameric, or heterotetrameric with PC1. PC2 shares a common transmembrane fold with other TRP channels, in addition to having a novel extracellular domain. Several TRP channels have been suggested to be regulated by lipids, including phosphatidylinositol phosphates (PIPs). We have combined molecular dynamics simulations with cryoelectron microscopy to explore possible lipid interactions sites on PC2. We propose that PC2 has a PIP-binding site close to the equivalent vanilloid/lipid-binding site in the TRPV1 channel. A 3.0 Å cryoelectron microscopy map reveals a binding site for cholesterol on PC2. Cholesterol interactions with the channel at this site are further characterized by MD simulations. These results help to position PC2 within an emerging model of the complex roles of lipids in the regulation and organization of ciliary membranes.

scholarly journals Photoaffinity labeling the lipid binding site of mammalian diacylglycerol kinase

2013 ◽  
Vol 27 (S1) ◽  
Author(s):  
Elizabeth Jane Petro ◽  
Becky Tu‐Sekine ◽  
Meng M. Rowland ◽  
Sammy Eni Eni ◽  
Michael D. Best ◽  
...  
Keyword(s):  
Binding Site ◽  
Photoaffinity Labeling ◽  
Diacylglycerol Kinase ◽  
Lipid Binding ◽  
Lipid Binding Site
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