Template:STRUCTURE 1ain

Annexins are proteins which make a membrane scaffold. They bind negatively charged phospholipids and contain a 70 amino acid long annexin repeat. They consist of 2 domains - the C-terminal core and the N-terminal head. 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. In the annexin image calcium ions are shown as green balls.

3D structures of annexin3D structures of annexin

Updated on 24-August-2014

Annexin IAnnexin I

2q4c, 1ycn - AnI - Arabidopsis thaliana
1mcx, 1hm6 - pAnI - pig
1qls - pAnI head+calgizzarrin
1bo9 - hAnI head - human NMR
1ain - hAnI
4mdv, 4mdu – AnI + Ca – Schistosoma mansoni

Annexin IIAnnexin II

2hyu, 2hyv - hAnII+heparin oligosaccharide
2hyw, 1xjl - hAnII+Ca
1w7b - hAnII
1bt6 - hAnII head+calpactin light chain

Annexin IIIAnnexin III

1aii, 1axn - hAnIII

Annexin IVAnnexin IV

2zhi, 2zhj, rAnIV+Na - rat
2zoc - hAnIV
1i4a - cAnIV (mutant) - cow
1aow, 1ann - cAnIV

Annexin VAnnexin V

2ie6, 2ie7, rAnV
1n41, 1n42, 1n44, 2h0k, 2h0l, 2h0m, 1bc0, 1bc1, 1bc3, 1bcw, 1bcy, 1bcz - rAnV (mutant)
1g5n - rAnV+ heparin oligosaccharide
1a8a, 1a8b - rAnV+phospholipid analog
2ran - rAnV+Ca
1yii – chAnV+Ca – chicken
1yj0 - chAnV+Zn
1ala - ChAnV
1hak - hAnV+K-201
1sav - hAnV (thioproline)
1hvd, 1hve, 1hvf, 1hvg - hAnV (mutant)
1anw, 1avh, 1avr - hAnV
1anx - hAnV+Ca
2xo2 – hAnV + Ca + azidohomoalanine
2xo3 - hAnV + Ca + homopropargylglycine

Annexin VIAnnexin VI

1m9i - hAnVI (mutant)
1avc - cAnVI+Ca

Annexin VIIIAnnexin VIII

1w3w - hAnVIII
1w45 - hAnVIII (mutant)

Annexin XIIAnnexin XII

1dm5 - HvAnXII (mutant) - Hydra vulgaris
1aei - HvAnXII

Annexin E1Annexin E1

3chj – GlAnE1 – Giardia lamblia
3chk, 3chl – GlAnE1 + cation

Other annexinsOther annexins

1dk5 - An24 - Capsicom annuum
3brx - coAnGH1+Ca - cotton
1n00 - coAnGH1

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

Alexander Berchansky, Michal Harel, Jaime Prilusky