Annexin: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
Annexins consist of 2 domains - the C-terminal core and the N-terminal head. | Annexins consist of 2 domains - the C-terminal core and the N-terminal head. The <scene name='41/410357/Cv/9'>core domain consists of 4 annexin repeats</scene> containing <scene name='41/410357/Cv/10'>5 helices</scene>. The core domain concave side contains the <scene name='41/410357/Cv/11'>Ca+2 binding sites</scene>.<ref>PMID:12401794</ref> | ||
</StructureSection> | </StructureSection> | ||
Revision as of 13:55, 6 January 2019
FunctionAnnexins 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. RelevanceAnnexin I is involved in anti-inflammatory responses and apoptotic mechanisms. Structural highlightsAnnexins consist of 2 domains - the C-terminal core and the N-terminal head. The containing . The core domain concave side contains the .[1]
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3D structures of annexin3D structures of annexin
Updated on 06-January-2019
ReferencesReferences
- ↑ 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