Secondary structure prediction of liver microsomal cytochrome P-450; proposed model of spatial arrangement in a membrane
Jazyk angličtina Země Nizozemsko Médium print
Typ dokumentu časopisecké články
PubMed
3401494
DOI
10.1016/0167-4838(88)90216-6
PII: 0167-4838(88)90216-6
Knihovny.cz E-zdroje
- MeSH
- algoritmy MeSH
- chemické modely * MeSH
- enzymová indukce MeSH
- fenobarbital farmakologie MeSH
- izoenzymy MeSH
- jaterní mikrozomy účinky léků enzymologie MeSH
- konformace proteinů MeSH
- králíci MeSH
- membrány enzymologie MeSH
- methylcholanthren farmakologie MeSH
- systém (enzymů) cytochromů P-450 * biosyntéza MeSH
- zvířata MeSH
- Check Tag
- králíci MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- fenobarbital MeSH
- izoenzymy MeSH
- methylcholanthren MeSH
- systém (enzymů) cytochromů P-450 * 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.
Citace poskytuje Crossref.org
