A database of predicted binding sites for cholesterol on membrane proteins, deep in the membrane
A database of predicted binding sites for cholesterol on membrane proteins, deep in the membrane
The outer membranes of animal cells contain high concentrations of cholesterol, of which a small proportion is located deep within the hydrophobic core of the membrane. An automated docking procedure is described that allows the characterization of binding sites for these deep cholesterol molecules on the membrane-spanning surfaces of membrane proteins and in protein cavities or pores, driven by hydrogen bond formation. A database of this class of predicted binding site is described, covering 397 high-resolution structures. The database includes sites on the transmembrane surfaces of many G-protein coupled receptors; within the fenestrations of two-pore K+ channels and ATP-gated P2X3 channels; in the central cavities of a number of transporters, including Glut1, Glut5, and P-glycoprotein; and in deep clefts in mitochondrial complexes III and IV.
Lee, Anthony G.
0891914c-e0e2-4ee1-b43e-1b70eb072d8e
Lee, Anthony G.
0891914c-e0e2-4ee1-b43e-1b70eb072d8e
Lee, Anthony G.
(2018)
A database of predicted binding sites for cholesterol on membrane proteins, deep in the membrane.
Biophysical Journal.
(doi:10.1016/j.bpj.2018.06.022).
Abstract
The outer membranes of animal cells contain high concentrations of cholesterol, of which a small proportion is located deep within the hydrophobic core of the membrane. An automated docking procedure is described that allows the characterization of binding sites for these deep cholesterol molecules on the membrane-spanning surfaces of membrane proteins and in protein cavities or pores, driven by hydrogen bond formation. A database of this class of predicted binding site is described, covering 397 high-resolution structures. The database includes sites on the transmembrane surfaces of many G-protein coupled receptors; within the fenestrations of two-pore K+ channels and ATP-gated P2X3 channels; in the central cavities of a number of transporters, including Glut1, Glut5, and P-glycoprotein; and in deep clefts in mitochondrial complexes III and IV.
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Accepted/In Press date: 19 June 2018
e-pub ahead of print date: 26 June 2018
Identifiers
Local EPrints ID: 422614
URI: http://eprints.soton.ac.uk/id/eprint/422614
ISSN: 0006-3495
PURE UUID: 194e089e-13b0-4766-9b4e-e55735005e36
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Date deposited: 26 Jul 2018 16:30
Last modified: 15 Mar 2024 21:01
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