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[[Image:1ain.png|left|200px|thumb|Crystal Structure of Human Annexin I, [[1ain]]]]
<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'>
{{STRUCTURE_1ain|  PDB=1ain  | SIZE=400| SCENE=Annexin/Cv/2 |right|CAPTION=Human Annexin I complex with Ca+2 ions, [[1ain]] }}
__TOC__
== 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>
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
[[Annexin|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 annexin==
==3D structures of annexin==
 
[[Annexin 3D structures]]
''Update May 2012''
 
== Annexin I ==
 
[[2q4c]], [[1ycn]] - AnI - ''Arabidopsis thaliana''<br />
[[1mcx]], [[1hm6]] - pAnI - pig<br />
[[1qls]] - pAnI head+calgizzarrin<br />
[[1bo9]] - hAnI head - human NMR<br />
[[1ain]] - hAnI<br />
 
== Annexin II ==
 
[[2hyu]], [[2hyv]] - hAnII+heparin oligosaccharide<br />
[[2hyw]], [[1xjl]] - hAnII+Ca<br />
[[1w7b]] - hAnII<br />
[[1bt6]] - hAnII head+calpactin light chain<br />
 
== Annexin III ==
 
[[1aii]], [[1axn]] - hAnIII<br />
 
== Annexin IV ==
 
[[2zhi]], [[2zhj]], rAnIV+Na - rat<br />
[[2zoc]] - hAnIV<br />
[[1i4a]] - cAnIV (mutant) - cow<br />
[[1aow]], [[1ann]] - cAnIV<br />
 
== Annexin V ==
 
[[2ie6]], [[2ie7]], rAnV<br />
[[1n41]], [[1n42]], [[1n44]], [[2h0k]], [[2h0l]], [[2h0m]], [[1bc0]], [[1bc1]], [[1bc3]], [[1bcw]], [[1bcy]], [[1bcz]]  - rAnV (mutant)<br />
[[1g5n]] - rAnV+ heparin oligosaccharide<br />
[[1a8a]], [[1a8b]] - rAnV+phospholipid analog<br />
[[2ran]] - rAnV+Ca<br />
[[1yii]] – chAnV+Ca – chicken<br />
[[1yj0]] - chAnV+Zn<br />
[[1ala]] - ChAnV<br />
[[1hak]] - hAnV+K-201<br />
[[1sav]] - hAnV (thioproline)<br />
[[1hvd]], [[1hve]], [[1hvf]], [[1hvg]] - hAnV (mutant)<br />
[[1anw]], [[1avh]], [[1avr]] - hAnV<br />
[[1anx]] - hAnV+Ca<br />
[[2xo2]] – hAnV + Ca + azidohomoalanine<br />
[[2xo3]] - hAnV + Ca + homopropargylglycine
 
== Annexin VI ==
 
[[1m9i]] - hAnVI (mutant)<br />
[[1avc]] - cAnVI+Ca<br />
 
== Annexin VIII ==
 
[[1w3w]] - hAnVIII<br />
[[1w45]] - hAnVIII (mutant)<br />
 
== Annexin XII ==
 
[[1dm5]] - HvAnXII (mutant) - ''Hydra vulgaris''<br />
[[1aei]] - HvAnXII<br />
 
== Annexin E1 ==
 
[[3chj]] – GlAnE1 – ''Giardia lamblia''<br />
[[3chk]], [[3chl]] – GlAnE1 + cation


== Other annexins ==
</StructureSection>


[[1dk5]] - An24 - ''Capsicom annuum''<br />
[[3brx]] - coAnGH1+Ca - cotton<br />
[[1n00]] - coAnGH1<br />


== References ==
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 12:58, 26 May 2024

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 I is involved in a variety of pathways[1].
  • Annexin II is involved in angiogenesis, tutor progression and metastasis[2]. See also Ezetimibe.

  • Annexin V is the most abundant scaffolding protein.
  • Annexin VI is involved in endocytosis and regulates entry of ligands to prelysosomal compartment[3].
  • Annexin VIII is calcium-dependent phospholipid-binding involved in blood coagulation[4].
  • 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.

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 .[5]

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. ↑ Lim LH, Pervaiz S. Annexin 1: the new face of an old molecule. FASEB J. 2007 Apr;21(4):968-75. PMID:17215481 doi:10.1096/fj.06-7464rev
  2. ↑ Sharma MC, Sharma M. The role of annexin II in angiogenesis and tumor progression: a potential therapeutic target. Curr Pharm Des. 2007;13(35):3568-75. PMID:18220793 doi:10.2174/138161207782794167
  3. ↑ Grewal T, Heeren J, Mewawala D, Schnitgerhans T, Wendt D, Salomon G, Enrich C, Beisiegel U, Jäckle S. Annexin VI stimulates endocytosis and is involved in the trafficking of low density lipoprotein to the prelysosomal compartment. J Biol Chem. 2000 Oct 27;275(43):33806-13. PMID:10940299 doi:10.1074/jbc.M002662200
  4. ↑ Sarkar A, Yang P, Fan YH, Mu ZM, Hauptmann R, Adolf GR, Stass SA, Chang KS. Regulation of the expression of annexin VIII in acute promyelocytic leukemia. Blood. 1994 Jul 1;84(1):279-86 PMID:8018923
  5. ↑ 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

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