View source for Annexin

<StructureSection load='1n42' size='350' side='right' caption='Rat annexin V complex with Ca+2 (green) and sulfate (PDB code [[1n42]])' scene='41/410357/Cv/3'>
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== 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 I''' is involved in a variety of pathways<ref>PMID:17215481</ref>. <br /> 
*'''Annexin II''' is involved in angiogenesis, tutor progression and metastasis<ref>PMID:18220793</ref>. See also [[Ezetimibe]].<br /><br />
*'''Annexin V''' is the most abundant scaffolding protein. <br />
*'''Annexin VI''' is involved in endocytosis and regulates entry of ligands to prelysosomal compartment<ref>PMID:10940299</ref>. <br /> 
*'''Annexin VIII''' is calcium-dependent phospholipid-binding involved in blood coagulation<ref>PMID:8018923</ref>. <br /> 
*'''Annexin E1''' (AnE1) is associated with tubulin in trophozoites of ''Giardia lamblia'' and forms local slubs in the flagella. <br />
*'''Annexin A-V''' has a major role in coagulation.  <br />

== 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 <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>

==3D structures of annexin==
[[Annexin 3D structures]]

</StructureSection>


== References ==
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