Title |
Molecular dynamics simulations indicate an induced-fit mechanism for LSD1/CoREST-H3-histone molecular recognition
|
---|---|
Published in |
BMC Biophysics, November 2013
|
DOI | 10.1186/2046-1682-6-15 |
Pubmed ID | |
Authors |
Nadeem A Vellore, Riccardo Baron |
Abstract |
Lysine Specific Demethylase (LSD1 or KDM1A) in complex with its co-repressor protein CoREST catalyzes the demethylation of the H3 histone N-terminal tail and is currently one of the most promising epigenetic targets for drug discovery against cancer and neurodegenerative diseases. Models of non-covalent binding, such as lock and key, induced-fit, and conformational selection could help explaining the molecular mechanism of LSD1/CoREST-H3-histone association, thus guiding drug discovery and design efforts. Here, we quantify the extent to which LSD1/CoREST substrate binding is consistent with these hypothetical models using LSD1/CoREST conformational ensembles obtained through extensive explicit solvent molecular dynamics (MD) simulations. |
X Demographics
Geographical breakdown
Country | Count | As % |
---|---|---|
Kenya | 1 | 50% |
Unknown | 1 | 50% |
Demographic breakdown
Type | Count | As % |
---|---|---|
Members of the public | 1 | 50% |
Practitioners (doctors, other healthcare professionals) | 1 | 50% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Italy | 2 | 5% |
Iran, Islamic Republic of | 1 | 3% |
China | 1 | 3% |
United States | 1 | 3% |
Unknown | 34 | 87% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Researcher | 10 | 26% |
Student > Ph. D. Student | 9 | 23% |
Student > Master | 4 | 10% |
Student > Bachelor | 3 | 8% |
Other | 3 | 8% |
Other | 6 | 15% |
Unknown | 4 | 10% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 14 | 36% |
Chemistry | 8 | 21% |
Biochemistry, Genetics and Molecular Biology | 6 | 15% |
Medicine and Dentistry | 2 | 5% |
Computer Science | 1 | 3% |
Other | 3 | 8% |
Unknown | 5 | 13% |