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 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

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 .[1]

3D structures of annexin

Annexin 3D structures


Rat annexin V complex with Ca+2 (green) and sulfate (PDB code 1n42)

Drag the structure with the mouse to rotate


ReferencesReferences

  1. 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel, Jaime Prilusky