Chapter title |
Hybrid In Silico/In Vitro Approaches for the Identification of Functional Cholesterol-Binding Domains in Membrane Proteins
|
---|---|
Chapter number | 2 |
Book title |
Cholesterol Homeostasis
|
Published in |
Methods in molecular biology, February 2017
|
DOI | 10.1007/978-1-4939-6875-6_2 |
Pubmed ID | |
Book ISBNs |
978-1-4939-6873-2, 978-1-4939-6875-6
|
Authors |
Coralie Di Scala, Jacques Fantini, Di Scala, Coralie, Fantini, Jacques, Scala, Coralie |
Editors |
Ingrid C. Gelissen, Andrew J. Brown |
Abstract |
In eukaryotic cells, cholesterol is an important regulator of a broad range of membrane proteins, including receptors, transporters, and ion channels. Understanding how cholesterol interacts with membrane proteins is a difficult task because structural data of these proteins complexed with cholesterol are scarce. Here, we describe a dual approach based on in silico studies of protein-cholesterol interactions, combined with physico-chemical measurements of protein insertion into cholesterol-containing monolayers. Our algorithm is validated through careful analysis of the effect of key mutations within and outside the predicted cholesterol-binding site. Our method is illustrated by a complete analysis of cholesterol-binding to Alzheimer's β-amyloid peptide, a protein that penetrates the plasma membrane of brain cells through a cholesterol-dependent process. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
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Unknown | 14 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
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Other | 2 | 14% |
Student > Master | 2 | 14% |
Student > Ph. D. Student | 2 | 14% |
Student > Postgraduate | 2 | 14% |
Researcher | 2 | 14% |
Other | 1 | 7% |
Unknown | 3 | 21% |
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Decision Sciences | 1 | 7% |
Other | 3 | 21% |
Unknown | 4 | 29% |