Annexins
| Annexins | ||
|---|---|---|
|
||
| Ribbon model of human Annexin-III according to PDB 1AXN | ||
| Mass / length primary structure | 310-350 amino acids | |
| Secondary to quaternary structure | Homotrimer, homohexamer | |
| Identifier | ||
| Gene name (s) | ANXA1 , ANXA2 , ANXA3 , ANXA4 , ANXA5 , ANXA6 , ANXA7 , ANXA8 , ANXA9 , ANXA10 , ANXA11 , ANXA13 | |
| Transporter classification | ||
| TCDB | 1.A.31 | |
| designation | Annexins | |
| Occurrence | ||
| Parent taxon | Eukaryotes | |
Annexins is the name of a family of proteins in eukaryotes whose common feature is the ability to bind to lipids in the cell membrane in a calcium-dependent manner and to assemble to form trimers or hexamers. Hexamers then usually form ion channel - transport proteins . Over 100 annexins in 45 species have now been sequenced, 12 of them in humans. Other names are lipocortin , synexin or endonexin .
The typical annexin protein is characterized by two key properties. Its polypeptide chain is folded into four repeated (or eight in Annexin VI) α-helical domains of similar structure with a central hydrophobic core. The second characteristic is the formation of calcium-dependent bonds to phospholipids , especially to acidic phospholipids, which have one or more negative charges.
The group of annexins is one of the two important calcium-binding proteins, plus the group of calmodulins .
literature
- McNeil AK, Rescher U, Gerke V, McNeil PL: Requirement for annexin A1 in plasma membrane repair . In: J. Biol. Chem. . 281, No. 46, November 2006, pp. 35202-7. doi : 10.1074 / jbc.M606406200 . PMID 16984915 .