Secondary structure prediction of liver microsomal cytochrome P-450; proposed model of spatial arrangement in a membrane
Language English Country Netherlands Media print
Document type Journal Article
PubMed
3401494
DOI
10.1016/0167-4838(88)90216-6
PII: 0167-4838(88)90216-6
Knihovny.cz E-resources
- MeSH
- Algorithms MeSH
- Models, Chemical * MeSH
- Enzyme Induction MeSH
- Phenobarbital pharmacology MeSH
- Isoenzymes MeSH
- Microsomes, Liver drug effects enzymology MeSH
- Protein Conformation MeSH
- Rabbits MeSH
- Membranes enzymology MeSH
- Methylcholanthrene pharmacology MeSH
- Cytochrome P-450 Enzyme System * biosynthesis MeSH
- Animals MeSH
- Check Tag
- Rabbits MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Phenobarbital MeSH
- Isoenzymes MeSH
- Methylcholanthrene MeSH
- Cytochrome P-450 Enzyme System * MeSH
The secondary structure of rabbit liver microsomal cytochrome P-450 LM2, rat liver microsomal cytochromes P-450b and P-450e (phenobarbital-inducible), and rat liver microsomal cytochromes P-450c, P-450d (3-methylcholanthrene-inducible) was predicted by a combination of methods (i) identifying the transmembrane parts of integral membrane proteins, and (ii) statistically predicting the secondary structure of globular proteins. The results are similar for all phenobarbital-inducible enzymes and make it possible to construct two structural models with seven or four transmembrane alpha-helices. The cytochromes of the second group obviously form a second structural family with four membrane-spanning alpha-helices. In both cases, a large ectodomain with several consecutive alpha-helices, which may provide the heme-binding pocket, is exposed out of the membrane.
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