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Homology models of human all-trans retinoic acid metabolizing enzymes CYP26B1 and CYP26B1 spliced-variant.

Saenz Mendez, Patricia (author)
Computational Chemistry and Biology Group, Facultad de Química, Universidad de la República (UdelaR), Montevideo, Uruguay
Elmabsout, Ali Ateia, 1977- (author)
Örebro universitet,Institutionen för hälsovetenskap och medicin,Department of Clinical Medicine, School of Health and Medical Sciences, Örebro University, Örebro, Sweden
Sävenstrand, Helena, 1974- (author)
Örebro universitet,Institutionen för naturvetenskap och teknik,Örebro Universitet
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Awadalla, M.K.A. (author)
Department of Clinical Medicine, School of Health Sciences, Örebro University, Örebro, Sweden
Strid, Åke, 1960- (author)
Örebro universitet,Institutionen för naturvetenskap och teknik,Biokemi,Örebro Universitet
Sirsjö, Allan, 1959- (author)
Örebro universitet,Institutionen för hälsovetenskap och medicin,Department of Clinical Medicine, School of Health and Medical Sciences, Örebro University, Örebro, Sweden
Eriksson, Leif A, 1964 (author)
Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology,Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden,Göteborgs Universitet
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 (creator_code:org_t)
2012-09-25
2012
English.
In: Journal of Chemical Information and Modeling. - Washington, USA : American Chemical Society (ACS). - 1549-9596 .- 1549-960X. ; 52:10, s. 2631-2637
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  • Journal article (peer-reviewed)
Abstract Subject headings
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  • Homology models of CYP26B1 (cytochrome P450RAI2) and CYP26B1 spliced variant were derived using the crystal structure of cyanobacterial CYP120A1 as template for the model building. The quality of the homology models generated were carefully evaluated, and the natural substrate all-trans-retinoic acid (atRA), several tetralone-derived retinoic acid metabolizing blocking agents (RAMBAs), and a well-known potent inhibitor of CYP26B1 (R115866) were docked into the homology model of full-length cytochrome P450 26B1. The results show that in the model of the full-length CYP26B1, the protein is capable of distinguishing between the natural substrate (atRA), R115866, and the tetralone derivatives. The spliced variant of CYP26B1 model displays a reduced affinity for atRA compared to the full-length enzyme, in accordance with recently described experimental information.

Subject headings

NATURVETENSKAP  -- Kemi (hsv//swe)
NATURAL SCIENCES  -- Chemical Sciences (hsv//eng)
NATURVETENSKAP  -- Biologi -- Bioinformatik och systembiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Bioinformatics and Systems Biology (hsv//eng)
NATURVETENSKAP  -- Kemi -- Teoretisk kemi (hsv//swe)
NATURAL SCIENCES  -- Chemical Sciences -- Theoretical Chemistry (hsv//eng)
NATURVETENSKAP  -- Kemi -- Fysikalisk kemi (hsv//swe)
NATURAL SCIENCES  -- Chemical Sciences -- Physical Chemistry (hsv//eng)
NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
NATURVETENSKAP  -- Data- och informationsvetenskap -- Bioinformatik (hsv//swe)
NATURAL SCIENCES  -- Computer and Information Sciences -- Bioinformatics (hsv//eng)

Keyword

Biochemistry

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