Behavior of Human Cytochromes P450 on Lipid Membranes
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F13%3A33145675" target="_blank" >RIV/61989592:15310/13:33145675 - isvavai.cz</a>
Alternative codes found
RIV/61989592:15110/13:33145675
Result on the web
<a href="http://pubs.acs.org/doi/abs/10.1021/jp4059559" target="_blank" >http://pubs.acs.org/doi/abs/10.1021/jp4059559</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/jp4059559" target="_blank" >10.1021/jp4059559</a>
Alternative languages
Result language
angličtina
Original language name
Behavior of Human Cytochromes P450 on Lipid Membranes
Original language description
Human cytochromes P450 (CYPs) are membrane-anchored enzymes involved in biotransformation of many marketed drugs. We constructed atomic models of six human CYPs (CYP1A2, 2A6, 2C9, 2D6, 2E1, and 3A4) anchored to a lipid bilayer to investigate the positions and orientations of CYPs on a membrane. We equilibrated the models by molecular dynamics simulations on a 100+ ns time scale. Catalytic domains of all studied CYPs were found to be partially immersed in the lipid bilayer, whereas the N-terminal part and F'/G' loop are deeply immersed The proximal side of the enzyme faces the cytosol, whereas the distal side, where openings of substrate access and product release channels to the active site are primarily located, points toward the lipid bilayer. Accesschannels with openings in the vicinity of the B/C and FIG loops are typically positioned below the lipid head groups, whereas the solvent channel points toward the membrane water interface. We found that the access channel opening positi
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
FR - Pharmacology and apothecary chemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach
Others
Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Physical Chemistry B
ISSN
1520-6106
e-ISSN
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Volume of the periodical
117
Issue of the periodical within the volume
39
Country of publishing house
US - UNITED STATES
Number of pages
9
Pages from-to
11556-11564
UT code for WoS article
000326301000016
EID of the result in the Scopus database
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