Annexin
From Proteopedia
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== Function == | == Function == | ||
| - | [[Annexin|Annexins]] are proteins which make a membrane scaffold. They bind negatively charged phospholipids and contain a 70 amino acid long annexin repeat. Annexins divide into species and are numbered from I to XII. '''Annexin V''' is the most abundant scaffolding protein. '''Annexin E1''' (AnE1) is associated with tubulin in trophozoites of ''Giardia lamblia'' and forms local slubs in the flagella. '''Annexin A-V''' has a major role in coagulation. '''Annexin AII''' has a major role in fibrinolysis. Annexins bind phospholipids and Ca+2 ions. | + | [[Annexin|Annexins]] are proteins which make a membrane scaffold. They bind negatively charged phospholipids and contain a 70 amino acid long annexin repeat. Annexins divide into species and are numbered from I to XII. '''Annexin V''' is the most abundant scaffolding protein. '''Annexin E1''' (AnE1) is associated with tubulin in trophozoites of ''Giardia lamblia'' and forms local slubs in the flagella. '''Annexin A-V''' has a major role in coagulation. '''Annexin AII''' has a major role in fibrinolysis. Annexins bind phospholipids and Ca+2 ions. See also [[Ezetimibe]]. |
== Relevance == | == Relevance == | ||
Revision as of 08:29, 28 February 2024
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References
- ↑ Mo Y, Campos B, Mealy TR, Commodore L, Head JF, Dedman JR, Seaton BA. Interfacial basic cluster in annexin V couples phospholipid binding and trimer formation on membrane surfaces. J Biol Chem. 2003 Jan 24;278(4):2437-43. Epub 2002 Oct 24. PMID:12401794 doi:10.1074/jbc.M210286200
