Sequence anatomy of mitochondrial anion carriers
Language English Country England, Great Britain Media print
Document type Journal Article, Research Support, Non-U.S. Gov't, Review
PubMed
12527356
DOI
10.1016/s0014-5793(02)03779-1
PII: S0014579302037791
Knihovny.cz E-resources
- MeSH
- Cytosol metabolism MeSH
- Protein Conformation MeSH
- Conserved Sequence MeSH
- Humans MeSH
- Mitochondria metabolism MeSH
- Anion Transport Proteins chemistry genetics metabolism MeSH
- Amino Acid Sequence MeSH
- Sequence Analysis, Protein MeSH
- Protein Structure, Tertiary MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Review MeSH
- Names of Substances
- Anion Transport Proteins MeSH
Two hundred and eighty-four genes of eight eukaryotic genomes for mitochondrial anion carriers were sorted into 43 (+18 single protein) subfamilies. Subfamilies differ by the number, nature, and locations of charges and polar residues in the transmembrane alpha-helices. Consequently, these residues and the rarely unique residues of the matrix and cytosolic segments most likely determine the different molecular phenotypes (functions). 'Common ancestral hydrophilic segments' were found in matrix and cytosolic segments, with interchangeable polar residues. Thus the hydrophobic microstructures of hydrophilic carrier parts are supposed to predetermine structure/conformation, whereas polar and charged microstructures should predetermine function, namely in the transmembrane spanning alpha-helices.
References provided by Crossref.org
Mitochondrial Uncoupling Proteins: Subtle Regulators of Cellular Redox Signaling
Channel character of uncoupling protein-mediated transport
