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Structure and dynamics of the membrane-bound cytochrome P450 2C9.

Abstract:

The microsomal, membrane-bound, human cytochrome P450 (CYP) 2C9 is a liver-specific monooxygenase essential for drug metabolism. CYPs require electron transfer from the membrane-bound CYP reductase (CPR) for catalysis. The structural details and functional relevance of the CYP-membrane interaction are not understood. From multiple coarse grained molecular simulations started with arbitrary configurations of protein-membrane complexes, we found two predominant orientations of CYP2C9 in the mem...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1371/journal.pcbi.1002152

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Institution:
University of Oxford
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
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Funding agency for:
Balali-Mood, K
Sansom, M
Grant:
WT083547MA
WT083547MA
More from this funder
Funding agency for:
Balali-Mood, K
Sansom, M
Grant:
WT083547MA
WT083547MA
Publisher:
Public Library of Science Publisher's website
Journal:
PLoS computational biology Journal website
Volume:
7
Issue:
8
Article number:
e1002152
Publication date:
2011-08-01
DOI:
EISSN:
1553-7358
ISSN:
1553-734X
Source identifiers:
175480
Language:
English
Keywords:
UUID:
uuid:98042bdf-4801-43d9-acab-06611f43d040
Local pid:
pubs:175480
Deposit date:
2012-12-19

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