Mechanism of lipid-protein interaction in the plasma lipoproteins: identification of a lipid-binding site in apolipoprotein A-II

Biochemistry ◽  
1981 ◽  
Vol 20 (6) ◽  
pp. 1676-1680 ◽  
Author(s):  
Simon J. T. Mao ◽  
Richard L. Jackson ◽  
Antonio M. Gotto ◽  
James T. Sparrow
Biochemistry ◽  
1977 ◽  
Vol 16 (19) ◽  
pp. 4150-4156 ◽  
Author(s):  
S. J. T. Mao ◽  
J. T. Sparrow ◽  
E. B. Gilliam ◽  
A. M. Gotto ◽  
R. L. Jackson

1991 ◽  
pp. 83-86
Author(s):  
Yifat Ziq-Bachar ◽  
David Levartowsky ◽  
Mordechaipras ◽  
Alistair F. Strachan ◽  
Mati Fridkin ◽  
...  

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

2008 ◽  
Vol 1778 (11) ◽  
pp. 2612-2620 ◽  
Author(s):  
Aleksander Czogalla ◽  
Krzysztof Grzymajło ◽  
Adam Jezierski ◽  
Aleksander F. Sikorski

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
David J. Wright ◽  
Katie J. Simmons ◽  
Rachel M. Johnson ◽  
David J. Beech ◽  
Stephen P. Muench ◽  
...  

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.


2005 ◽  
Vol 89 (6) ◽  
pp. 4081-4089 ◽  
Author(s):  
Phedra Marius ◽  
Simon J. Alvis ◽  
J. Malcolm East ◽  
Anthony G. Lee

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