Annexin: Difference between revisions
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{{STRUCTURE_1ain| PDB=1ain | SIZE=400| SCENE=Annexin/Cv/2 |right|CAPTION=Human annexin I complex with Ca+2 ions, [[1ain]] }} | {{STRUCTURE_1ain| PDB=1ain | SIZE=400| SCENE=Annexin/Cv/2 |right|CAPTION=Human annexin I complex with Ca+2 ions, [[1ain]] }} | ||
<StructureSection load='1n42' size='340' side='right' caption='Tyrosine aminomutase complex with peptide-derived chromophore cofactor (PDB code [[1n42]])' scene=''> | |||
== 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. | ||
== Relevance == | |||
Annexin I is involved in anti-inflammatory responses and apoptotic mechanisms. | |||
== 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 core domain consists of 4 annexin repeats containing 5 helices. The core domain concave side contains the Ca+2 binding sites. | ||
==3D structures of annexin== | ==3D structures of annexin== | ||