Annexin

Function

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 I is involved in a variety of pathways.
Annexin V is the most abundant scaffolding ^[1]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

Annexin I is involved in anti-inflammatory responses and apoptotic mechanisms.

Structural highlights

Annexins consist of 2 domains - the C-terminal core and the N-terminal head. The containing . The core domain concave side contains the .^[2]

3D structures of annexin

Annexin 3D structures

ReferencesReferences

↑ Lim LH, Pervaiz S. Annexin 1: the new face of an old molecule. FASEB J. 2007 Apr;21(4):968-75. PMID:17215481 doi:10.1096/fj.06-7464rev
↑ 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

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[1] Lim LH, Pervaiz S. Annexin 1: the new face of an old molecule. FASEB J. 2007 Apr;21(4):968-75. PMID:17215481 doi:10.1096/fj.06-7464rev

[2] 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

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